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Volumn 22, Issue 5, 2003, Pages 465-478

Antimicrobial peptides in animals and their role in host defences

Author keywords

Anionic peptides; Antimicrobial peptides; Cathelicidins; Cationic peptides; Defensins; Domesticated animals; Innate defence; Livestock

Indexed keywords

ALPHA DEFENSIN; ANION; ANTIINFECTIVE AGENT; BETA DEFENSIN; CATHELICIDIN; CATHELIN; CATION; CECROPIN; CECROPIN P1; CYSTEINE DERIVATIVE; DEFENSIN; INDOLICIDIN; PEPTIDE; PROLINE DERIVATIVE; PROPHENIN; PROTEGRIN; PROTEIN BAC5; PROTEIN BAC7; PROTEIN BNBD 1; PROTEIN BNBD 2; PROTEIN BNBD 3; PROTEIN BNBD 4; PROTEIN BNBD 5; PROTEIN BNBD 6; PROTEIN BNBD 7; PROTEIN BNBD 8; PROTEIN PR 39; PROTEIN SMAP29; SEMEN PLASMIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 0242353107     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0924-8579(03)00180-8     Document Type: Review
Times cited : (419)

References (141)
  • 1
    • 0033042407 scopus 로고    scopus 로고
    • Use of antimicrobial growth promoters in food animals and Enterococcus faecium resistance to therapeutic antimicrobial drugs in Europe
    • Wegener H.C., Aarestrup F.M., Jensen L.B., Hammerum A.M., Bager F. Use of antimicrobial growth promoters in food animals and Enterococcus faecium resistance to therapeutic antimicrobial drugs in Europe. Emerg. Infect. Dis. 5:1999;329-335.
    • (1999) Emerg. Infect. Dis. , vol.5 , pp. 329-335
    • Wegener, H.C.1    Aarestrup, F.M.2    Jensen, L.B.3    Hammerum, A.M.4    Bager, F.5
  • 2
    • 0032512458 scopus 로고    scopus 로고
    • Medical consequences of antibiotic use in agriculture
    • Witte W. Medical consequences of antibiotic use in agriculture. Science. 279:1998;996-997.
    • (1998) Science , vol.279 , pp. 996-997
    • Witte, W.1
  • 4
    • 0033772917 scopus 로고    scopus 로고
    • Antimicrobial-drug use and changes in resistance in Streptococcus pneumoniae
    • Diekema D.J., Brueggemann A.B., Doern G.V. Antimicrobial-drug use and changes in resistance in Streptococcus pneumoniae. Emerg. Infect. Dis. 6:2000;552-556.
    • (2000) Emerg. Infect. Dis. , vol.6 , pp. 552-556
    • Diekema, D.J.1    Brueggemann, A.B.2    Doern, G.V.3
  • 5
    • 0030628291 scopus 로고    scopus 로고
    • The contribution of antibiotic use on the frequency of antibiotic resistance in hospitals
    • Gaynes R., Monnet D. The contribution of antibiotic use on the frequency of antibiotic resistance in hospitals. Ciba Found Symp. 207:1997;47-56.
    • (1997) Ciba Found Symp. , vol.207 , pp. 47-56
    • Gaynes, R.1    Monnet, D.2
  • 6
    • 0031454283 scopus 로고    scopus 로고
    • The impact of antimicrobial use on the emergence of antimicrobial- resistant bacteria in hospitals
    • Gaynes R. The impact of antimicrobial use on the emergence of antimicrobial-resistant bacteria in hospitals. Infect. Dis. Clin. North Am. 11:1997;757-765.
    • (1997) Infect. Dis. Clin. North Am. , vol.11 , pp. 757-765
    • Gaynes, R.1
  • 7
    • 0033554074 scopus 로고    scopus 로고
    • Animal feed antibiotic use raises drug resistance fear
    • Marwick C. Animal feed antibiotic use raises drug resistance fear. J. Am. Med. Assoc. 282:1999;120-122.
    • (1999) J. Am. Med. Assoc. , vol.282 , pp. 120-122
    • Marwick, C.1
  • 8
    • 0035909656 scopus 로고    scopus 로고
    • Antimicrobial use in animal feed - Time to stop
    • Gorbach S.L. Antimicrobial use in animal feed - time to stop. N. Engl. J. Med. 345:2001;1202-1203.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1202-1203
    • Gorbach, S.L.1
  • 10
    • 0029961099 scopus 로고    scopus 로고
    • Antimicrobial-resistant pathogens in the 1990s
    • Jacoby G.A. Antimicrobial-resistant pathogens in the 1990s. Annu. Rev. Med. 47:1996;169-179.
    • (1996) Annu. Rev. Med. , vol.47 , pp. 169-179
    • Jacoby, G.A.1
  • 11
    • 0034098916 scopus 로고    scopus 로고
    • Bactericidal activity of mammalian cathelicidin-derived peptides
    • Travis S.M., Anderson N.N., Forsyth W.R., et al. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect. Immun. 68:2000;2748-2755.
    • (2000) Infect. Immun. , vol.68 , pp. 2748-2755
    • Travis, S.M.1    Anderson, N.N.2    Forsyth, W.R.3
  • 12
    • 0028289032 scopus 로고
    • Characterization of a rabbit cationic protein (CAP18) with lipopolysaccharide-inhibitory activity
    • Hirata M., Shimomura Y., Yoshida M., et al. Characterization of a rabbit cationic protein (CAP18) with lipopolysaccharide-inhibitory activity. Infect. Immun. 62:1994;1421-1426.
    • (1994) Infect. Immun. , vol.62 , pp. 1421-1426
    • Hirata, M.1    Shimomura, Y.2    Yoshida, M.3
  • 13
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variabe C-terminal antimicrobial domain
    • Zanetti M., Gennaro R., Romeo D. Cathelicidins: a novel protein family with a common proregion and a variabe C-terminal antimicrobial domain. FEBS Lett. 374:1995;1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 14
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo R.L., Kim K.J., Bernfield M., et al. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272:1997;13088-13093.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3
  • 15
    • 0031729624 scopus 로고    scopus 로고
    • Evaluation of antimicrobial and lipopolysaccharide-neutralizing effects of a synthetic CAP18 fragment against Pseudomonas aeruginosa in a mouse model
    • Sawa T., Kurahashi K., Ohara M., et al. Evaluation of antimicrobial and lipopolysaccharide-neutralizing effects of a synthetic CAP18 fragment against Pseudomonas aeruginosa in a mouse model. Antimicrob. Agents Chemother. 42:1998;3269-3275.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 3269-3275
    • Sawa, T.1    Kurahashi, K.2    Ohara, M.3
  • 16
    • 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. 13:1995;61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 17
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: Their function, structure, biogenesis, and mechanism of action
    • Nissen-Meyer J., Nes I.F. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch. Microbiol. 167:1997;67-77.
    • (1997) Arch. Microbiol. , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, I.F.2
  • 18
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer R.I., Ganz T. Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11:1999;23-27.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 19
    • 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
  • 20
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P., Mor A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbiol. 49:1995;277-304.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 21
    • 0026486781 scopus 로고
    • Ovine pulmonary surfactant induces killing of Pasteurella haemolytica, Escherichia coli, and Klebsiella pneumoniae by normal serum
    • Brogden K.A. Ovine pulmonary surfactant induces killing of Pasteurella haemolytica, Escherichia coli, and Klebsiella pneumoniae by normal serum. Infect. Immun. 60:1992;5182-5189.
    • (1992) Infect. Immun. , vol.60 , pp. 5182-5189
    • Brogden, K.A.1
  • 22
    • 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. 93:1996;412-416.
    • (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
  • 23
    • 0016670373 scopus 로고
    • The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships
    • de Haen C., Neurath H., Teller D.C. The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships. J. Mol. Biol. 92:1975;225-259.
    • (1975) J. Mol. Biol. , vol.92 , pp. 225-259
    • De Haen, C.1    Neurath, H.2    Teller, D.C.3
  • 24
    • 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. 41:1997;1615-1617.
    • (1997) Antimicrob. Agents Chem. , vol.41 , pp. 1615-1617
    • Brogden, K.A.1    Ackermann, M.2    Huttner, K.M.3
  • 25
    • 0035038534 scopus 로고    scopus 로고
    • Comparison of bronchoalveolar lavage fluid obtained from Mannheimia haemolytica-inoculated calves with and without prior treatment with the selectin inhibitor TBC1269
    • Caverly J.M., Radi Z.A., Andreasen C.B., Dixon R.A., Brogden K.A., Ackermann M.R. Comparison of bronchoalveolar lavage fluid obtained from Mannheimia haemolytica-inoculated calves with and without prior treatment with the selectin inhibitor TBC1269. Am. J. Vet. Res. 62:2001;665-672.
    • (2001) Am. J. Vet. Res. , vol.62 , pp. 665-672
    • Caverly, J.M.1    Radi, Z.A.2    Andreasen, C.B.3    Dixon, R.A.4    Brogden, K.A.5    Ackermann, M.R.6
  • 26
    • 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. 66:1998;5948-5954.
    • (1998) Infect. Immun. , vol.66 , pp. 5948-5954
    • Brogden, K.A.1    Ackermann, M.2    Huttner, K.M.3
  • 27
    • 0017169432 scopus 로고
    • Bacterial growth inhibition by amniotic fluid. VI. Evidence for a zinc-peptide antibacterial system
    • Schlievert P., Johnson W., Galask R.P. Bacterial growth inhibition by amniotic fluid. VI. Evidence for a zinc-peptide antibacterial system. Am. J. Obstet. Gynecol. 125:1976;906-910.
    • (1976) Am. J. Obstet. Gynecol. , vol.125 , pp. 906-910
    • Schlievert, P.1    Johnson, W.2    Galask, R.P.3
  • 28
    • 0021889174 scopus 로고
    • Isolation of an antibacterial peptide from human lung lavage fluid
    • Ellison R.T. III, Boose D., LaForce F.M. Isolation of an antibacterial peptide from human lung lavage fluid. J. Infect. Dis. 151:1985;1123-1129.
    • (1985) J. Infect. Dis. , vol.151 , pp. 1123-1129
    • Ellison R.T. III1    Boose, D.2    LaForce, F.M.3
  • 29
    • 0021251715 scopus 로고
    • Effect of zinc and phosphate on an antibacterial peptide isolated from lung lavage
    • LaForce F.M., Boose D.S. Effect of zinc and phosphate on an antibacterial peptide isolated from lung lavage. Infect. Immun. 45:1984;692-696.
    • (1984) Infect. Immun. , vol.45 , pp. 692-696
    • LaForce, F.M.1    Boose, D.S.2
  • 30
    • 0242302216 scopus 로고
    • Zinc(II) complexes with aspartate and glutamate
    • Bottari E. Zinc(II) complexes with aspartate and glutamate. J. Coord. Chem. 21:1990;215-224.
    • (1990) J. Coord. Chem. , vol.21 , pp. 215-224
    • Bottari, E.1
  • 31
    • 0037653852 scopus 로고
    • An ultracentrifugal study of the efficiency of some macromolecular inhibitors of ribonuclease
    • Littauer U.Z., Sela M. An ultracentrifugal study of the efficiency of some macromolecular inhibitors of ribonuclease. Biochim. Biophys. Acta. 61:1962;609-611.
    • (1962) Biochim. Biophys. Acta , vol.61 , pp. 609-611
    • Littauer, U.Z.1    Sela, M.2
  • 32
    • 0007905908 scopus 로고
    • Inhibition of ribonuclease by copolymers of glutamic acid and aromatic amino acids
    • Sela M. Inhibition of ribonuclease by copolymers of glutamic acid and aromatic amino acids. J. Biol. Chem. 237:1962;418-421.
    • (1962) J. Biol. Chem. , vol.237 , pp. 418-421
    • Sela, M.1
  • 33
    • 84965187370 scopus 로고
    • Inhibitors of ribonuclease activity
    • Vandendriessche L. Inhibitors of ribonuclease activity. Arch. Biochem. Biophys. 65:1956;347-353.
    • (1956) Arch. Biochem. Biophys. , vol.65 , pp. 347-353
    • Vandendriessche, L.1
  • 34
    • 0030728214 scopus 로고    scopus 로고
    • Structural organization of the bovine cathelicidin gene family and identification of a novel member
    • Scocchi M., Wang S.L., Zanetti M. Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett. 417:1997;311-315.
    • (1997) FEBS Lett. , vol.417 , pp. 311-315
    • Scocchi, M.1    Wang, S.L.2    Zanetti, M.3
  • 36
    • 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. 55:2000;31-49.
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 37
    • 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. 34:1995;11479-11488.
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 38
    • 0030926012 scopus 로고    scopus 로고
    • Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine
    • Vunnam S., Juvvadi P., Merrifield R.B. Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine. J. Pept. Res. 49:1997;59-66.
    • (1997) J. Pept. Res. , vol.49 , pp. 59-66
    • Vunnam, S.1    Juvvadi, P.2    Merrifield, R.B.3
  • 39
    • 0024331982 scopus 로고
    • Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin
    • Lee J.-Y., Boman A., Chuanxin S., et al. Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin. Proc. Natl. Acad. Sci. USA. 86:1989;9159-9162.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9159-9162
    • Lee, J.-Y.1    Boman, A.2    Chuanxin, S.3
  • 40
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells
    • Zanetti M., Storici P., Tossi A., Scocchi M., Gennaro R. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. J. Biol. Chem. 269:1994;7855-7858.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7855-7858
    • Zanetti, M.1    Storici, P.2    Tossi, A.3    Scocchi, M.4    Gennaro, R.5
  • 41
    • 0034184327 scopus 로고    scopus 로고
    • Porcine antimicrobial peptides: New prospects for ancient molecules of host defense
    • Zhang G., Ross C.R., Blecha F. Porcine antimicrobial peptides: new prospects for ancient molecules of host defense. Vet. Res. 31:2000;277-296.
    • (2000) Vet. Res. , vol.31 , pp. 277-296
    • Zhang, G.1    Ross, C.R.2    Blecha, F.3
  • 42
    • 0034811573 scopus 로고    scopus 로고
    • Fungicidal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Candida albicans
    • Lee D.G., Kim D.H., Park Y., et al. Fungicidal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Candida albicans. Biochem. Biophys. Res. Commun. 282:2001;570-574.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 570-574
    • Lee, D.G.1    Kim, D.H.2    Park, Y.3
  • 44
    • 0028834275 scopus 로고
    • CDNA sequences of three sheep myeloid cathelicidins
    • Bagella L., Scocchi M., Zanetti M. cDNA sequences of three sheep myeloid cathelicidins. FEBS Lett. 376:1995;225-228.
    • (1995) FEBS Lett. , vol.376 , pp. 225-228
    • Bagella, L.1    Scocchi, M.2    Zanetti, M.3
  • 45
    • 0029584314 scopus 로고
    • Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide
    • Mahoney M.M., Lee A.Y., Brezinski-Caliguri D.J., Huttner K.M. Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide. FEBS Lett. 377:1995;519-522.
    • (1995) FEBS Lett. , vol.377 , pp. 519-522
    • Mahoney, M.M.1    Lee, A.Y.2    Brezinski-Caliguri, D.J.3    Huttner, K.M.4
  • 46
    • 0033433992 scopus 로고    scopus 로고
    • SMAP-29: A potent antibacterial and antifungal peptide from sheep leukocytes
    • Skerlavaj B., Benincasa M., Risso A., Zanetti M., Gennaro R. SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett. 463:1999;58-62.
    • (1999) FEBS Lett. , vol.463 , pp. 58-62
    • Skerlavaj, B.1    Benincasa, M.2    Risso, A.3    Zanetti, M.4    Gennaro, R.5
  • 47
    • 0034812782 scopus 로고    scopus 로고
    • Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis
    • Saiman L., Tabibi S., Starner T.D., et al. Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis. Antimicrob. Agents Chemother. 45:2001;2838-2844.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2838-2844
    • Saiman, L.1    Tabibi, S.2    Starner, T.D.3
  • 49
    • 0031725844 scopus 로고    scopus 로고
    • Biological characterization of a novel mammalian antimicrobial peptide
    • Gennaro R., Scocchi M., Merluzzi L., Zanetti M. Biological characterization of a novel mammalian antimicrobial peptide. Biochim. Biophys. Acta. 1425:1998;361-368.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 361-368
    • Gennaro, R.1    Scocchi, M.2    Merluzzi, L.3    Zanetti, M.4
  • 51
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins
    • Skerlavaj B, Romeo D, Gennaro R. Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins, Infect Immun 1990;58:3724-30.
    • (1990) Infect Immun , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 52
    • 0025065276 scopus 로고
    • Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils
    • Frank R.W., Gennaro R., Schneider K., Przybylski M., Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J. Biol. Chem. 265:1990;18871-18874.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18871-18874
    • Frank, R.W.1    Gennaro, R.2    Schneider, K.3    Przybylski, M.4    Romeo, D.5
  • 53
    • 0024460671 scopus 로고
    • Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils
    • Gennaro R., Skerlavaj B., Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect. Immun. 57:1989;3142-3146.
    • (1989) Infect. Immun. , vol.57 , pp. 3142-3146
    • Gennaro, R.1    Skerlavaj, B.2    Romeo, D.3
  • 54
    • 0032808386 scopus 로고    scopus 로고
    • Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes
    • Shamova O., Brogden K.A., Zhao C., Nguyen T., Kokryakov V.N., Lehrer R.I. Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. Infect. Immun. 67:1999;4106-4111.
    • (1999) Infect. Immun. , vol.67 , pp. 4106-4111
    • Shamova, O.1    Brogden, K.A.2    Zhao, C.3    Nguyen, T.4    Kokryakov, V.N.5    Lehrer, R.I.6
  • 55
    • 0032500067 scopus 로고    scopus 로고
    • Cloning and analysis of a transcript derived from two contiguous genes of the cathelicidin family
    • Scocchi M., Wang S.L., Gennaro R., Zanetti M. Cloning and analysis of a transcript derived from two contiguous genes of the cathelicidin family. Biochim. Biophys. Acta Gene Struct. Expr. 1398:1998;393-396.
    • (1998) Biochim. Biophys. Acta Gene Struct. Expr. , vol.1398 , pp. 393-396
    • Scocchi, M.1    Wang, S.L.2    Gennaro, R.3    Zanetti, M.4
  • 56
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics
    • Zanetti M., Del Sal G., Storici P., Schneider C., Romeo D. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268:1993;522-526.
    • (1993) J. Biol. Chem. , vol.268 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3    Schneider, C.4    Romeo, D.5
  • 57
    • 0025081012 scopus 로고
    • Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules
    • Zanetti M., Litteri L., Gennaro R., Horstmann H., Romeo D. Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules. J. Cell. Biol. 111:1990;1363-1371.
    • (1990) J. Cell. Biol. , vol.111 , pp. 1363-1371
    • Zanetti, M.1    Litteri, L.2    Gennaro, R.3    Horstmann, H.4    Romeo, D.5
  • 58
    • 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. 61:1993;2978-2984.
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 59
    • 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., Ross C.R., Chengappa M.M., Sylte M.J., McVey D.S., Blecha F. Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Antimicrob. Agents Chem. 40:1996;115-121.
    • (1996) Antimicrob. Agents Chem. , vol.40 , pp. 115-121
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Sylte, M.J.4    McVey, D.S.5    Blecha, F.6
  • 60
    • 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. 376:1995;130-134.
    • (1995) FEBS Lett. , vol.376 , pp. 130-134
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3
  • 62
    • 0028585933 scopus 로고
    • Identification of a proline-argining-rich antibacterial peptide from neutrophils that is analogous to PR-39, and antibacterial peptide from the small intestine
    • Shi J., Ross C.R., Chengappa M.M., Blecha F. Identification of a proline-argining-rich antibacterial peptide from neutrophils that is analogous to PR-39, and antibacterial peptide from the small intestine. J. Leukoc. Biol. 56:1994;807-811.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 807-811
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Blecha, F.4
  • 63
    • 0035001927 scopus 로고    scopus 로고
    • In vitro activity of PR-39, a proline-arginine-rich peptide, against susceptible and multi-drug-resistant Mycobacterium tuberculosis
    • Linde C.M., Hoffner S.E., Refai E., Andersson M. In vitro activity of PR-39, a proline-arginine-rich peptide, against susceptible and multi-drug-resistant Mycobacterium tuberculosis. J. Antimicrob. Chemother. 47:2001;575-580.
    • (2001) J. Antimicrob. Chemother. , vol.47 , pp. 575-580
    • Linde, C.M.1    Hoffner, S.E.2    Refai, E.3    Andersson, M.4
  • 64
    • 0035109873 scopus 로고    scopus 로고
    • Anti-microbial activity and cell binding are controlled by sequence determinants in the anti-microbial peptide PR-39
    • Chan Y.R., Zanetti M., Gennaro R., Gallo R.L. Anti-microbial activity and cell binding are controlled by sequence determinants in the anti-microbial peptide PR-39. J. Invest. Dermatol. 116:2001;230-235.
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 230-235
    • Chan, Y.R.1    Zanetti, M.2    Gennaro, R.3    Gallo, R.L.4
  • 65
    • 0034749320 scopus 로고    scopus 로고
    • PR-39, a proline/arginine-rich antimicrobial peptide, exerts cardioprotective effects in myocardial ischemia-reperfusion
    • Ikeda Y., Young L.H., Scalia R., Ross C.R., Lefer A.M. PR-39, a proline/arginine-rich antimicrobial peptide, exerts cardioprotective effects in myocardial ischemia-reperfusion. Cardiovasc. Res. 49:2001;69-77.
    • (2001) Cardiovasc. Res. , vol.49 , pp. 69-77
    • Ikeda, Y.1    Young, L.H.2    Scalia, R.3    Ross, C.R.4    Lefer, A.M.5
  • 66
    • 0030976983 scopus 로고    scopus 로고
    • Chemoattractant properties of PR-39, a neutrophil antibacterial peptide
    • Huang H.J., Ross C.R., Blecha F. Chemoattractant properties of PR-39, a neutrophil antibacterial peptide. J. Leukoc. Biol. 61:1997;624-629.
    • (1997) J. Leukoc. Biol. , vol.61 , pp. 624-629
    • Huang, H.J.1    Ross, C.R.2    Blecha, F.3
  • 68
    • 0029347029 scopus 로고
    • Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor
    • Strukelj B., Pungercar J., Kopitar G., et al. Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor. Biol. Chem. Hoppe-Seyler. 376:1995;507-510.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 507-510
    • Strukelj, B.1    Pungercar, J.2    Kopitar, G.3
  • 71
    • 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. 72:1997;794-805.
    • (1997) Biophys. J. , vol.72 , pp. 794-805
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 73
    • 0020562530 scopus 로고
    • Antibacterial activity of microbicidal cationic proteins 1 and 2, matural peptide antibiotics of rabbit lung macrophages
    • Lehrer R.I., Selsted M.E., Szklarek D., Fleischmann J. Antibacterial activity of microbicidal cationic proteins 1 and 2, matural peptide antibiotics of rabbit lung macrophages. Infect. Immun. 42:1983;10-14.
    • (1983) Infect. Immun. , vol.42 , pp. 10-14
    • Lehrer, R.I.1    Selsted, M.E.2    Szklarek, D.3    Fleischmann, J.4
  • 74
    • 0023945703 scopus 로고
    • Modulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations
    • Lehrer R.I., Ganz T., Szklarek D., Selsted M.E. Modulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations. J. Clin. Invest. 81:1988;1829-1835.
    • (1988) J. Clin. Invest. , vol.81 , pp. 1829-1835
    • Lehrer, R.I.1    Ganz, T.2    Szklarek, D.3    Selsted, M.E.4
  • 75
    • 0021792199 scopus 로고
    • Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes
    • Lehrer R.I., Daher K., Ganz T., Selsted M.E. Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes. J. Virol. 54:1985;467-472.
    • (1985) J. Virol. , vol.54 , pp. 467-472
    • Lehrer, R.I.1    Daher, K.2    Ganz, T.3    Selsted, M.E.4
  • 77
    • 0027514011 scopus 로고
    • Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils
    • Selsted M.E., Tang Y.-Q., Morris W.L., et al. Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils. Biol. Chem. 268:1993;6641-6648.
    • (1993) Biol. Chem. , vol.268 , pp. 6641-6648
    • Selsted, M.E.1    Tang, Y.-Q.2    Morris, W.L.3
  • 78
    • 0033543750 scopus 로고    scopus 로고
    • Cloning and expression of bovine neutrophil beta-defensins. Biosynthetic profile during neutrophilic maturation and localization of mature peptide to novel cytoplasmic dense granules
    • Yount N.Y., Yuan J., Tarver A., et al. Cloning and expression of bovine neutrophil beta-defensins. Biosynthetic profile during neutrophilic maturation and localization of mature peptide to novel cytoplasmic dense granules. J. Biol. Chem. 274:1999;26249-26258.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26249-26258
    • Yount, N.Y.1    Yuan, J.2    Tarver, A.3
  • 79
    • 0027414945 scopus 로고
    • Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils
    • Tang Y.Q., Selsted M.E. Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils. J. Biol. Chem. 268:1993;6649-6653.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6649-6653
    • Tang, Y.Q.1    Selsted, M.E.2
  • 80
    • 0031882530 scopus 로고    scopus 로고
    • Expression of beta-defensin genes in bovine alveolar macrophages
    • Ryan L.K., Rhodes J., Bhat M., Diamond G. Expression of beta-defensin genes in bovine alveolar macrophages. Infect. Immun. 66:1998;878-881.
    • (1998) Infect. Immun. , vol.66 , pp. 878-881
    • Ryan, L.K.1    Rhodes, J.2    Bhat, M.3    Diamond, G.4
  • 81
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA
    • Diamond G., Zasloff M., Eck H., Brasseur M., Maloy W.L., Bevins C.L. Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc. Natl. Acad. Sci. USA. 88:1991;3952-3956.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.L.5    Bevins, C.L.6
  • 83
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter B.S., Stolzenberg E.D., Zasloff M.A. Epithelial antibiotics induced at sites of inflammation. Science. 267:1995;1645-1648.
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 84
    • 0027298895 scopus 로고
    • Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene
    • Diamond G., Jones D.E., Bevins C.L. Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene. Proc. Natl. Acad. Sci. USA. 90:1993;4596-4600.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4596-4600
    • Diamond, G.1    Jones, D.E.2    Bevins, C.L.3
  • 85
    • 0028258347 scopus 로고
    • Endotoxin upregulates expression of an antimicrobial peptide gene in mammalian airway epithelial cells
    • Diamond G., Bevins C. Endotoxin upregulates expression of an antimicrobial peptide gene in mammalian airway epithelial cells. Chest. 105:1994;51S-52S.
    • (1994) Chest , vol.105
    • Diamond, G.1    Bevins, C.2
  • 86
    • 0031937280 scopus 로고    scopus 로고
    • Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract
    • Huttner K.M. Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract. Am. Soc. Nutr. Sci. 1998;297S-299S.
    • (1998) Am. Soc. Nutr. Sci.
    • Huttner, K.M.1
  • 87
    • 0030463889 scopus 로고    scopus 로고
    • High-resolution FISH mapping of β-defensin genes to river buffalo and sheep chromosomes suggests a chromosome discrepancy in cattle standard karyotypes
    • Iannuzzi L., Gallagher D.S., Di Meo G.P., Diamond G., Bevins C.L., Womack J.E. High-resolution FISH mapping of β-defensin genes to river buffalo and sheep chromosomes suggests a chromosome discrepancy in cattle standard karyotypes. Cytogenet. Cell. Genet. 75:1996;10-13.
    • (1996) Cytogenet. Cell. Genet. , vol.75 , pp. 10-13
    • Iannuzzi, L.1    Gallagher, D.S.2    Di Meo, G.P.3    Diamond, G.4    Bevins, C.L.5    Womack, J.E.6
  • 88
    • 0032709098 scopus 로고    scopus 로고
    • Differential expression of caprine β-defensins in digestive and respiratory tissues
    • Zhao C., Nguyen T., Liu L., Shamova O., Brogden K., Lehrer R.I. Differential expression of caprine β-defensins in digestive and respiratory tissues. Infect. Immun. 67:1999;6221-6224.
    • (1999) Infect. Immun. , vol.67 , pp. 6221-6224
    • Zhao, C.1    Nguyen, T.2    Liu, L.3    Shamova, O.4    Brogden, K.5    Lehrer, R.I.6
  • 89
    • 0033023402 scopus 로고    scopus 로고
    • Porcine epithelial β-defensin 1 is expressed in the dorsal tongue at antimicrobial concentrations
    • Shi J., Zhang G., Wu H., Ross C., Blecha F., Ganz T. Porcine epithelial β-defensin 1 is expressed in the dorsal tongue at antimicrobial concentrations. Infect. Immun. 67:1999;3121-3127.
    • (1999) Infect. Immun. , vol.67 , pp. 3121-3127
    • Shi, J.1    Zhang, G.2    Wu, H.3    Ross, C.4    Blecha, F.5    Ganz, T.6
  • 90
    • 0031694275 scopus 로고    scopus 로고
    • Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow
    • Brockus C.W., Jackwood M.W., Harmon B.G. Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow. Anim. Genet. 29:1998;283-289.
    • (1998) Anim. Genet. , vol.29 , pp. 283-289
    • Brockus, C.W.1    Jackwood, M.W.2    Harmon, B.G.3
  • 91
    • 0028211686 scopus 로고
    • Gallinacins: Cysteine-rich antimicrobial peptides of chicken leukocytes
    • Harwig S.S., Swiderek K.M., Kokryakov V.N., et al. Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes. FEBS Lett. 342:1994;281-285.
    • (1994) FEBS Lett. , vol.342 , pp. 281-285
    • Harwig, S.S.1    Swiderek, K.M.2    Kokryakov, V.N.3
  • 94
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang Y.Q., Yuan J., Osapay G., et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science. 286:1999;498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3
  • 95
    • 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
  • 96
    • 0032536098 scopus 로고    scopus 로고
    • Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study
    • Roumestand C., Louis V., Aumelas A., Grassy G., Calas B., Chavanieu A. Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study. FEBS Lett. 421:1998;263-267.
    • (1998) FEBS Lett. , vol.421 , pp. 263-267
    • Roumestand, C.1    Louis, V.2    Aumelas, A.3    Grassy, G.4    Calas, B.5    Chavanieu, A.6
  • 97
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryakov V.N., Harwig S.S., Panyutich E.A., et al. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327:1993;231-236.
    • (1993) FEBS Lett. , vol.327 , pp. 231-236
    • Kokryakov, V.N.1    Harwig, S.S.2    Panyutich, E.A.3
  • 98
    • 0031870993 scopus 로고    scopus 로고
    • The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids
    • Shi J.S., Ganz T. The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids. Infect. Immun. 66:1998;3611-3617.
    • (1998) Infect. Immun. , vol.66 , pp. 3611-3617
    • Shi, J.S.1    Ganz, T.2
  • 100
    • 0031115106 scopus 로고    scopus 로고
    • Antibacterial peptides of bovine lactoferrin: Purification and characterization
    • Dionysius D.A., Milne J.M. Antibacterial peptides of bovine lactoferrin: purification and characterization. J. Dairy Sci. 80:1997;667-674.
    • (1997) J. Dairy Sci. , vol.80 , pp. 667-674
    • Dionysius, D.A.1    Milne, J.M.2
  • 101
    • 0034877273 scopus 로고    scopus 로고
    • Bulky aromatic amino acids increase the antibacterial activity of 15-residue bovine lactoferricin derivatives
    • Haug B.E., Skar M.L., Svendsen J.S. Bulky aromatic amino acids increase the antibacterial activity of 15-residue bovine lactoferricin derivatives. J. Pept. Sci. 7:2001;425-432.
    • (2001) J. Pept. Sci. , vol.7 , pp. 425-432
    • Haug, B.E.1    Skar, M.L.2    Svendsen, J.S.3
  • 102
    • 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. 245:1998;764-773.
    • (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
  • 103
    • 0032437146 scopus 로고    scopus 로고
    • Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin
    • Kuwata H., Yip T.T., Tomita M., Hutchens T.W. Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin. Biochim. Biophys. Acta. 1429:1998;129-141.
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 129-141
    • Kuwata, H.1    Yip, T.T.2    Tomita, M.3    Hutchens, T.W.4
  • 104
    • 0035083899 scopus 로고    scopus 로고
    • A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils
    • Ueta E., Tanida T., Osaki T. A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. J. Pept. Res. 57:2001;240-249.
    • (2001) J. Pept. Res. , vol.57 , pp. 240-249
    • Ueta, E.1    Tanida, T.2    Osaki, T.3
  • 105
    • 0034684272 scopus 로고    scopus 로고
    • Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism
    • Ibrahim H.R., Sugimoto Y., Aoki T. Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim. Biophys. Acta. 1523:2000;196-205.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 196-205
    • Ibrahim, H.R.1    Sugimoto, Y.2    Aoki, T.3
  • 106
    • 0035002090 scopus 로고    scopus 로고
    • Suppression of Mannheimia (Pasteurella) haemolytica serovar 1 infection in lambs by intrapulmonary administration of ovine antimicrobial anionic peptide
    • Kalfa V.C., Palmquist D., Ackermann M.R., Brogden K.A. Suppression of Mannheimia (Pasteurella) haemolytica serovar 1 infection in lambs by intrapulmonary administration of ovine antimicrobial anionic peptide. Int. J. Antimicrob. Agents. 17:2001;505-510.
    • (2001) Int. J. Antimicrob. Agents , vol.17 , pp. 505-510
    • Kalfa, V.C.1    Palmquist, D.2    Ackermann, M.R.3    Brogden, K.A.4
  • 110
    • 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. Isolation and characterization of human β-Defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276:2001;5707-5713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 111
    • 0035941493 scopus 로고    scopus 로고
    • Discovery of new human b-defensins using a genomics-based approach
    • In press
    • Jia HP, Schutte BC, Schudy A et al. Discovery of new human b-defensins using a genomics-based approach, Gene 2001; In press.
    • (2001) Gene
    • Jia, H.P.1    Schutte, B.C.2    Schudy, A.3
  • 112
    • 0035430147 scopus 로고    scopus 로고
    • Human b-defensin 4: A novel inducible peptide with a specific salt- sensitive spectrum of antimicrobial activity
    • Garcia J.R., Krause A., Schulz S., et al. Human b-defensin 4: a novel inducible peptide with a specific salt- sensitive spectrum of antimicrobial activity. FASEB J. 15:2001;1819-1821.
    • (2001) FASEB J. , vol.15 , pp. 1819-1821
    • Garcia, J.R.1    Krause, A.2    Schulz, S.3
  • 114
    • 0036127867 scopus 로고    scopus 로고
    • Lactoferrin inhibits hepatitis C virus viremia in chronic hepatitis C patients with high viral loads and HCV genotype 1b
    • Iwasa M., Kaito M., Ikoma J., et al. Lactoferrin inhibits hepatitis C virus viremia in chronic hepatitis C patients with high viral loads and HCV genotype 1b. Am. J. Gastroenterol. 97:2002;766-767.
    • (2002) Am. J. Gastroenterol. , vol.97 , pp. 766-767
    • Iwasa, M.1    Kaito, M.2    Ikoma, J.3
  • 116
    • 0036250985 scopus 로고    scopus 로고
    • Large scale production of recombinant human lactoferrin in the milk of transgenic cows
    • van Berkel P.H., Welling M.M., Geerts M., et al. Large scale production of recombinant human lactoferrin in the milk of transgenic cows. Nat. Biotechnol. 20:2002;484-487.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 484-487
    • Van Berkel, P.H.1    Welling, M.M.2    Geerts, M.3
  • 117
    • 0034028209 scopus 로고    scopus 로고
    • 13-Week oral repeated administration toxicity study of bovine lactoferrin in rats
    • Yamauchi K., Toida T., Nishimura S., et al. 13-Week oral repeated administration toxicity study of bovine lactoferrin in rats. Food Chem. Toxicol. 38:2000;503-512.
    • (2000) Food Chem. Toxicol. , vol.38 , pp. 503-512
    • Yamauchi, K.1    Toida, T.2    Nishimura, S.3
  • 118
    • 0024842051 scopus 로고
    • Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo
    • Zagulski T., Lipinski P., Zagulska A., Broniek S., Jarzabek Z. Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo. Br. J. Exp. Pathol. 70:1989;697-704.
    • (1989) Br. J. Exp. Pathol. , vol.70 , pp. 697-704
    • Zagulski, T.1    Lipinski, P.2    Zagulska, A.3    Broniek, S.4    Jarzabek, Z.5
  • 120
    • 0037911520 scopus 로고    scopus 로고
    • Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease
    • Brogden K.A., Heidari M., Sacco R.E., et al. Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease. Oral Microbiol. Immunol. 18:2003;95-99.
    • (2003) Oral Microbiol. Immunol. , vol.18 , pp. 95-99
    • Brogden, K.A.1    Heidari, M.2    Sacco, R.E.3
  • 121
    • 0031036742 scopus 로고    scopus 로고
    • Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin
    • Sitaram N., Subbalakshmi C., Krishnakumari V., Nagaraj R. Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin. FEBS Lett. 400:1997;289-292.
    • (1997) FEBS Lett. , vol.400 , pp. 289-292
    • Sitaram, N.1    Subbalakshmi, C.2    Krishnakumari, V.3    Nagaraj, R.4
  • 122
    • 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. 11:1993;105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 123
    • 15644370080 scopus 로고    scopus 로고
    • Enteric beta defensin: Molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection
    • Tarver A.P., Clark D.P., Diamond G., et al. Enteric beta defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection. Infect. Immun. 66:1998;1045-1056.
    • (1998) Infect. Immun. , vol.66 , pp. 1045-1056
    • Tarver, A.P.1    Clark, D.P.2    Diamond, G.3
  • 124
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj B., Gennaro R., Bagella L., Merluzzi L., Risso A., Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271:1996;28375-28381.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 125
    • 0028031219 scopus 로고
    • Molecular cloning of Bac7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils
    • Scocchi M., Romeo D., Zanetti M. Molecular cloning of Bac7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils. FEBS Lett. 352:1994;197-200.
    • (1994) FEBS Lett. , vol.352 , pp. 197-200
    • Scocchi, M.1    Romeo, D.2    Zanetti, M.3
  • 126
    • 0026448914 scopus 로고
    • CDNA sequence analysis of an antibiotic dodecapeptide from neutrophils
    • Storici P., Del Sal G., Schneider C., Zanetti M. cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils. FEBS Lett. 314:1992;187-190.
    • (1992) FEBS Lett. , vol.314 , pp. 187-190
    • Storici, P.1    Del Sal, G.2    Schneider, C.3    Zanetti, M.4
  • 127
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo D., Skerlavaj B., Bolognesi M., Gennaro R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263:1988;9573-9575.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 128
    • 0032484654 scopus 로고    scopus 로고
    • Localization and genomic organization of sheep antimicrobial peptide genes
    • Huttner K.M., Lambeth M.R., Burkin H.R., Burkin D.J., Broad T.E. Localization and genomic organization of sheep antimicrobial peptide genes. Gene. 206:1998;85-91.
    • (1998) Gene , vol.206 , pp. 85-91
    • Huttner, K.M.1    Lambeth, M.R.2    Burkin, H.R.3    Burkin, D.J.4    Broad, T.E.5
  • 129
    • 0032489350 scopus 로고    scopus 로고
    • Molecular cloning and tissue expression of porcine b-defensin-1
    • Zhang G., Wu H., Shi J., Ganz T., Ross C.R., Blecha F. Molecular cloning and tissue expression of porcine b-defensin-1. FEBS Lett. 424:1998;37-40.
    • (1998) FEBS Lett. , vol.424 , pp. 37-40
    • Zhang, G.1    Wu, H.2    Shi, J.3    Ganz, T.4    Ross, C.R.5    Blecha, F.6
  • 130
    • 0028009472 scopus 로고
    • Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA
    • Storici P., Scocchi M., Tossi A., Gennaro R., Zanetti M. Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA. FEBS Lett. 337:1994;303-307.
    • (1994) FEBS Lett. , vol.337 , pp. 303-307
    • Storici, P.1    Scocchi, M.2    Tossi, A.3    Gennaro, R.4    Zanetti, M.5
  • 131
    • 0028904007 scopus 로고
    • PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity
    • Tossi A., Scocchi M., Zanetti M., Storici P., Gennaro R. PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity. Eur. J. Biochem. 228:1995;941-946.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 941-946
    • Tossi, A.1    Scocchi, M.2    Zanetti, M.3    Storici, P.4    Gennaro, R.5
  • 132
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth B., Lee J.Y., Bergman T., et al. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem. 202:1991;849-854.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.Y.2    Bergman, T.3
  • 133
    • 0030252539 scopus 로고    scopus 로고
    • Prophenin and PR39X - Novel antimicrobial leukocyte peptides regulating functional activity of thrombocytes
    • Tkachenko S.B., Kokriakov V.N., Ashmarin I.P., Kubatiev A.A. Prophenin and PR39X - novel antimicrobial leukocyte peptides regulating functional activity of thrombocytes. Dokl. Akad. Nauk. 350:1996;704-706.
    • (1996) Dokl. Akad. Nauk. , vol.350 , pp. 704-706
    • Tkachenko, S.B.1    Kokriakov, V.N.2    Ashmarin, I.P.3    Kubatiev, A.A.4
  • 134
    • 0029015666 scopus 로고
    • The structure of porcine protegrin genes
    • Zhao C., Ganz T., Lehrer R.I. The structure of porcine protegrin genes. FEBS Lett. 368:1995;197-202.
    • (1995) FEBS Lett. , vol.368 , pp. 197-202
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3
  • 135
    • 0026689270 scopus 로고
    • Identification of eNAP-1, an antimicrobial peptide from equine neutrophils
    • Couto M.A., Harwig S.S., Cullor J.S., Hughes J.P., Lehrer R.I. Identification of eNAP-1, an antimicrobial peptide from equine neutrophils. Infect. Immun. 60:1992;3065-3071.
    • (1992) Infect. Immun. , vol.60 , pp. 3065-3071
    • Couto, M.A.1    Harwig, S.S.2    Cullor, J.S.3    Hughes, J.P.4    Lehrer, R.I.5
  • 136
    • 0031694275 scopus 로고    scopus 로고
    • Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow
    • Brockus C.W., Jackwood M.W., Harmon B.G. Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow. Anim. Genet. 29:1998;283-289.
    • (1998) Anim. Genet. , vol.29 , pp. 283-289
    • Brockus, C.W.1    Jackwood, M.W.2    Harmon, B.G.3
  • 138
    • 0028263457 scopus 로고
    • Identification of a new member of the protegrin family by cDNA cloning
    • Zhao C., Liu L., Lehrer R.I. Identification of a new member of the protegrin family by cDNA cloning. FEBS Lett. 346:1994;285-288.
    • (1994) FEBS Lett. , vol.346 , pp. 285-288
    • Zhao, C.1    Liu, L.2    Lehrer, R.I.3
  • 139
    • 0032709098 scopus 로고    scopus 로고
    • Differential expression of caprine b-defensins in digestive and respiratory tissues
    • Zhao C., Nguyen T., Liu L., Shamova O., Brogden K., Lehrer R.I. Differential expression of caprine b-defensins in digestive and respiratory tissues. Infect. Immun. 67:1999;6221-6224.
    • (1999) Infect. Immun. , vol.67 , pp. 6221-6224
    • Zhao, C.1    Nguyen, T.2    Liu, L.3    Shamova, O.4    Brogden, K.5    Lehrer, R.I.6
  • 140
    • 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. 85:1988;5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 141
    • 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. 87:1990;210-214.
    • (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


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