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Volumn 9, Issue 4, 1998, Pages 269-280

β-sheet antibiotic peptides as potential dental therapeutics

Author keywords

Antibiotic peptides; Defensins; Oral; Periodontal; Protegrins; Therapeutics

Indexed keywords

ANDROPIN; ANTIBIOTIC AGENT; BACTENECIN; CECROPIN; CLAVANIN; CYSTEINE; DEFENSIN; MAGAININ DERIVATIVE; PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; TACHYPLESIN; UNCLASSIFIED DRUG;

EID: 0031925507     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0924-8579(98)00006-5     Document Type: Article
Times cited : (65)

References (81)
  • 1
    • 0028239445 scopus 로고
    • Ubiquitous natural antibiotics
    • Gabay J.E. Ubiquitous natural antibiotics. Science. 264:1994;373-374.
    • (1994) Science , vol.264 , pp. 373-374
    • Gabay, J.E.1
  • 2
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock R.E. Peptide antibiotics. Lancet. 349:1997;418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 4
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman H.G. Antibacterial peptides: Key components needed in immunity. Cell. 65:1991;205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 5
    • 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
  • 7
    • 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., Hostmann 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    Hostmann, H.4    Romeo, D.5
  • 8
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • Casteels P., Ampe C., Jacob F., Vaeck M., Tempst P. Apidaecins: Antibacterial peptides from honeybees. EMBO J. 8:1989;2387-2391.
    • (1989) EMBO J , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacob, F.3    Vaeck, M.4    Tempst, P.5
  • 9
    • 0029929079 scopus 로고    scopus 로고
    • Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide of Drosophila
    • Bulet P., Urge L., Ohresser S., Hetru C., Otvos L. Jr. Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide of Drosophila. Eur J Biochem. 238:1996;64-69.
    • (1996) Eur J Biochem , vol.238 , pp. 64-69
    • Bulet, P.1    Urge, L.2    Ohresser, S.3    Hetru, C.4    Otvos L., Jr.5
  • 10
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug, Pyrrhocoris apterus
    • Cociancich S., Dupont A., Hegy G. et al. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug, Pyrrhocoris apterus. Biochem J. 300:1994;567-575.
    • (1994) Biochem J , vol.300 , pp. 567-575
    • Cociancich, S.1    Dupont, A.2    Hegy, G.3
  • 11
    • 0029051008 scopus 로고
    • A novel antibacterial peptide family isolated from the silkworm, Bombyx mori
    • Hara S., Yamakawa M. A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem J. 310:1995;651-656.
    • (1995) Biochem J , vol.310 , pp. 651-656
    • Hara, S.1    Yamakawa, M.2
  • 12
    • 0025058306 scopus 로고
    • Isolation and characterization of abaecin, major antibacterial response peptide in the honeybee (Apis mellifera)
    • Casteels P., Ampe C., Riviere L. et al. Isolation and characterization of abaecin, major antibacterial response peptide in the honeybee (Apis mellifera). Eur J Biochem. 187:1990;381-386.
    • (1990) Eur J Biochem , vol.187 , pp. 381-386
    • Casteels, P.1    Ampe, C.2    Riviere, L.3
  • 13
    • 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
  • 14
    • 0029989651 scopus 로고    scopus 로고
    • Delineation of an active fragment and poly(L-proline) II conformation for candidacidal activity of bactenecin 5
    • Raj P.A., Marcus E., Edgerton M. Delineation of an active fragment and poly(L-proline) II conformation for candidacidal activity of bactenecin 5. Biochemistry. 35:1996;4314-4325.
    • (1996) Biochemistry , vol.35 , pp. 4314-4325
    • Raj, P.A.1    Marcus, E.2    Edgerton, M.3
  • 15
    • 0025065276 scopus 로고
    • Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides from bovine neutrophils
    • Frank R.W., Gennaro R., Schneider K., Przybylski M., Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides from 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
  • 16
    • 0028905203 scopus 로고
    • Interaction of the fragments characteristic of bactenecin 7 with phospholipid bilayers and their antimicrobial activity
    • Tani A., Lee S., Oishi O., Aoyagi H., Ohno M. Interaction of the fragments characteristic of bactenecin 7 with phospholipid bilayers and their antimicrobial activity. J Biochem. 117:1995;560-565.
    • (1995) J Biochem , vol.117 , pp. 560-565
    • Tani, A.1    Lee, S.2    Oishi, O.3    Aoyagi, H.4    Ohno, M.5
  • 17
  • 18
    • 0025780002 scopus 로고
    • A family of bombinin-related peptides from the skin of Bombina variegate
    • Simmaco M., Barra D., Chiarini F. et al. A family of bombinin-related peptides from the skin of Bombina variegate. Eur J Biochem. 199:1991;217-222.
    • (1991) Eur J Biochem , vol.199 , pp. 217-222
    • Simmaco, M.1    Barra, D.2    Chiarini, F.3
  • 19
    • 0025372569 scopus 로고
    • All-D amino acid-containing channel forming antibiotic peptides
    • Wade D., Boman A., Wåhlin B. et al. All-D amino acid-containing channel forming antibiotic peptides. Proc Natl Acad Sci USA. 87:1990;4761-4765.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4761-4765
    • Wade, D.1    Boman, A.2    Wåhlin, B.3
  • 20
    • 0023692422 scopus 로고
    • Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrine
    • Matsuyama K., Natori S. Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrine. J Biol Chem. 263:1988;17112-17116.
    • (1988) J Biol Chem , vol.263 , pp. 17112-17116
    • Matsuyama, K.1    Natori, S.2
  • 21
    • 0025959246 scopus 로고
    • The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster
    • Samakovlis C., Kylsten P., Kimbrell D.A., Engström Å., Hultmark D. The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster. EMBO J. 10:1991;163-169.
    • (1991) EMBO J , vol.10 , pp. 163-169
    • Samakovlis, C.1    Kylsten, P.2    Kimbrell, D.A.3    Engström, Å.4    Hultmark, D.5
  • 22
    • 0026445022 scopus 로고
    • The use of capillary electrophoresis to identify cationic proteins in human parotid saliva
    • Lal K., Xu L., Colburn J., Hong A.L., Pollock J.J. The use of capillary electrophoresis to identify cationic proteins in human parotid saliva. Arch Oral Biol. 37:1992;713.
    • (1992) Arch Oral Biol , vol.37 , pp. 713
    • Lal, K.1    Xu, L.2    Colburn, J.3    Hong, A.L.4    Pollock, J.J.5
  • 23
    • 0030570839 scopus 로고    scopus 로고
    • Stabilization of helix by side-chain interactions in histatin-derived peptides: Role in candidacidal activity
    • Ramalingam K., Gururaja T.L., Ramasubbu N., Levine M.J. Stabilization of helix by side-chain interactions in histatin-derived peptides: Role in candidacidal activity. Biochem Biophys Res Commun. 225:1996;47-53.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 47-53
    • Ramalingam, K.1    Gururaja, T.L.2    Ramasubbu, N.3    Levine, M.J.4
  • 24
    • 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
  • 25
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T., Furanaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S. Tachyplesin, a class of antimicrobial peptide from 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    Furanaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6
  • 26
    • 0025078937 scopus 로고
    • Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the β-sheet structure
    • Kawano K., Yoneya T., Miyata T. et al. Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the β-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
  • 27
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: Chemical structures and biologic activity
    • Miyata T., Tokunaga F., Yoneya T. et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: Chemical structures and biologic activity. J Biochem. 106:1989;663-668.
    • (1989) J Biochem , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3
  • 28
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryakov V.N., Harwig S.S.L., 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.L.2    Panyutich, E.A.3
  • 29
    • 0027197728 scopus 로고
    • Purlfication and characterization of a scorpion defensin, a 42 kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins
    • Cociancich S., Goyffon M., Bontems F. et al. Purlfication and characterization of a scorpion defensin, a 42 kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins. Biochem Biophys Res Commun. 194:1993;17-22.
    • (1993) Biochem Biophys Res Commun , vol.194 , pp. 17-22
    • Cociancich, S.1    Goyffon, M.2    Bontems, F.3
  • 30
    • 0026738576 scopus 로고
    • Insect defensins: Inducible antibacterial peptides
    • Hoffmann J.A., Hetru C. Insect defensins: Inducible antibacterial peptides. Immunol Today. 13:1992;411-415.
    • (1992) Immunol Today , vol.13 , pp. 411-415
    • Hoffmann, J.A.1    Hetru, C.2
  • 31
    • 20244363184 scopus 로고
    • Insect immunity: Isolation from immune blood of dipteran Phomia terranovae of two insect antibacterial peptides with sequence homology to rabbit macrophage bactericidal peptides
    • Lambert J., Keppi E., Dimarcq J.-L. et al. Insect immunity: Isolation from immune blood of dipteran Phomia terranovae of two insect antibacterial peptides with sequence homology to rabbit macrophage bactericidal peptides. Proc Natl Acad Sci USA. 86:1989;262-266.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 262-266
    • Lambert, J.1    Keppi, E.2    Dimarcq, J.-L.3
  • 32
    • 0024289191 scopus 로고
    • Molecular cloning of cDNA for sapecin and unique expression of the sapecin gene during the development of Sarcophaga peregrina
    • Matsuyama K., Natori S. Molecular cloning of cDNA for sapecin and unique expression of the sapecin gene during the development of Sarcophaga peregrina. J Biol Chem. 263:1988;17117-17121.
    • (1988) J Biol Chem , vol.263 , pp. 17117-17121
    • Matsuyama, K.1    Natori, S.2
  • 33
    • 0025311318 scopus 로고
    • A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin
    • Fujiwara S., Imai J., Fujiwara M., Yaeshima T., Kawashima T., Kobayashi K. A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. J Biol Chem. 265:1990;11333-11337.
    • (1990) J Biol Chem , vol.265 , pp. 11333-11337
    • Fujiwara, S.1    Imai, J.2    Fujiwara, M.3    Yaeshima, T.4    Kawashima, T.5    Kobayashi, K.6
  • 34
    • 0029948648 scopus 로고    scopus 로고
    • Isolation and characterization of a new member of the insect defensin family from a beetle, Allomyrina dichotoma
    • Miyanoshita A., Hara S., Sugiyama M. et al. Isolation and characterization of a new member of the insect defensin family from a beetle, Allomyrina dichotoma. Biochem Biophys Res Commun. 220:1996;526-531.
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 526-531
    • Miyanoshita, A.1    Hara, S.2    Sugiyama, M.3
  • 36
    • 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. J Biol Chem. 268:1993;6641-6648.
    • (1993) J Biol Chem , vol.268 , pp. 6641-6648
    • Selsted, M.E.1    Tang, Y.-Q.2    Morris, W.L.3
  • 37
    • 0027414945 scopus 로고
    • Characterization of the distilfide motif in BNBD-12, an antimicrobial β-defensin peptide from bovine neutrophils
    • Tang Y.-Q., Selsted M.E. Characterization of the distilfide motif in BNBD-12, an antimicrobial β-defensin peptide from bovine neutrophils. J Biol Chem. 268:1993;6849-6853.
    • (1993) J Biol Chem , vol.268 , pp. 6849-6853
    • Tang, Y.-Q.1    Selsted, M.E.2
  • 38
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa:peptide isolation and cloning of 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 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
  • 39
    • 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
  • 41
    • 0030569343 scopus 로고    scopus 로고
    • Widespread expression of β-defensin hBD-1 in human secretory cells and epithelial cells
    • Zhao C., Wang I., Lehrer R.I. Widespread expression of β-defensin hBD-1 in human secretory cells and epithelial cells. FEBS Lett. 396:1996;319-322.
    • (1996) FEBS Lett , vol.396 , pp. 319-322
    • Zhao, C.1    Wang, I.2    Lehrer, R.I.3
  • 42
    • 0028211686 scopus 로고
    • Gallinacins: Cysteine-rich antimicrobial peptides of chicken leukocytes
    • Harwig S.S.L., 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.L.1    Swiderek, K.M.2    Kokryakov, V.N.3
  • 43
    • 0021142387 scopus 로고
    • Purlfication and antibacterial activity of antimicrobial peptides of rabbit granulocytes
    • Selsted M.E., Szklarek D., Lehrer R.I. Purlfication and antibacterial activity of antimicrobial peptides of rabbit granulocytes. Infect Immun. 45:1984;150-154.
    • (1984) Infect Immun , vol.45 , pp. 150-154
    • Selsted, M.E.1    Szklarek, D.2    Lehrer, R.I.3
  • 44
    • 0026712324 scopus 로고
    • Cryptdins: Antimicrobial defensins of the murine small intestine
    • Eisenhauer P.B., Harwig S.S.L., Lehrer R.I. Cryptdins: Antimicrobial defensins of the murine small intestine. Infect Immun. 60:1992;3556-3565.
    • (1992) Infect Immun , vol.60 , pp. 3556-3565
    • Eisenhauer, P.B.1    Harwig, S.S.L.2    Lehrer, R.I.3
  • 45
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones D.E., Bevins C.L. Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem. 267:1992;23216-23225.
    • (1992) J Biol Chem , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 46
    • 0023270758 scopus 로고
    • Purification, primary structure, and antimicrobial activities of the guinea pig neutrophil defensin
    • Selsted M.E., Harwig S.S.L. Purification, primary structure, and antimicrobial activities of the guinea pig neutrophil defensin. Infect Immun. 55:1987;2281-2286.
    • (1987) Infect Immun , vol.55 , pp. 2281-2286
    • Selsted, M.E.1    Harwig, S.S.L.2
  • 49
    • 0030997215 scopus 로고    scopus 로고
    • Improved activity of a synthetic indolicidin analog
    • Falla T.J., Hancock R.E. Improved activity of a synthetic indolicidin analog. Antimicrob Agents Chemother. 41:1997;771-775.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 771-775
    • Falla, T.J.1    Hancock, R.E.2
  • 50
    • 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
  • 51
    • 0027144508 scopus 로고
    • Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells
    • Radermacher S.W., Schoop V.M., Schluesener H.J. Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells. J Neurosci Res. 36:1993;657-662.
    • (1993) J Neurosci Res , vol.36 , pp. 657-662
    • Radermacher, S.W.1    Schoop, V.M.2    Schluesener, H.J.3
  • 52
    • 0029851698 scopus 로고    scopus 로고
    • Candidacidal activity of recombinant human salivary histatin-5 and variants
    • Tsai H., Raj P.A., Bobek L.A. Candidacidal activity of recombinant human salivary histatin-5 and variants. Infect Immun. 64:1996;5000-5007.
    • (1996) Infect Immun , vol.64 , pp. 5000-5007
    • Tsai, H.1    Raj, P.A.2    Bobek, L.A.3
  • 53
    • 0022402545 scopus 로고
    • Defensins. Natural peptide antibiotics of human neutrophils
    • Ganz T., Selsted M.E., Szklarek D. et al. Defensins. Natural peptide antibiotics of human neutrophils. J Clin Invest. 76:1985;1427-1435.
    • (1985) J Clin Invest , vol.76 , pp. 1427-1435
    • Ganz, T.1    Selsted, M.E.2    Szklarek, D.3
  • 54
    • 0026652575 scopus 로고
    • Cationic defensins arise from chargeneutralized propeptides: A mechanism for avoiding leukocyte autotoxicity?
    • Michaelson D., Rayner J., Couto M., Ganz T. Cationic defensins arise from chargeneutralized propeptides: A mechanism for avoiding leukocyte autotoxicity? J Leukocyte Biol. 51:1992;634-639.
    • (1992) J Leukocyte Biol , vol.51 , pp. 634-639
    • Michaelson, D.1    Rayner, J.2    Couto, M.3    Ganz, T.4
  • 56
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner H., Andreu D., Merrifield R.B. Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects. Biochim Biophys Acta. 939:1988;260-266.
    • (1988) Biochim Biophys Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 57
    • 0027528472 scopus 로고
    • Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera)
    • Casteels P., Ampe C., Jacobs F., Tempst P. Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J Biol Chem. 268:1993;7044-7054.
    • (1993) J Biol Chem , vol.268 , pp. 7044-7054
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Tempst, P.4
  • 58
    • 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
  • 60
    • 0025690257 scopus 로고
    • Sensitivity of oral, Gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins
    • Miyasaki K.T., Bodeau A.L., Ganz T., Selsted M.E., Lehrer R.I. Sensitivity of oral, Gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins. Infect Immun. 58:1990;3934-3940.
    • (1990) Infect Immun , vol.58 , pp. 3934-3940
    • Miyasaki, K.T.1    Bodeau, A.L.2    Ganz, T.3    Selsted, M.E.4    Lehrer, R.I.5
  • 61
    • 0026056095 scopus 로고
    • Differential killing of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. by human neutrophil granule components
    • Miyasaki K.T., Bodeau A.L., Flemmig T.F. Differential killing of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. by human neutrophil granule components. Infect Immun. 59:1991;3760-3767.
    • (1991) Infect Immun , vol.59 , pp. 3760-3767
    • Miyasaki, K.T.1    Bodeau, A.L.2    Flemmig, T.F.3
  • 62
    • 0024601077 scopus 로고
    • A salmonella locus that controls resistance to microbicidal proteins from phagocytic cells
    • Fields P.I., Groisman E.A., Heffron F. A salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science. 243:1989;1059-1062.
    • (1989) Science , vol.243 , pp. 1059-1062
    • Fields, P.I.1    Groisman, E.A.2    Heffron, F.3
  • 63
    • 0025096413 scopus 로고
    • Characterization of defensin resistance phenotypes associated with mutations in the phoP virulence regulon of Salmonella typhimurium
    • Miller S.I., Pulkkinen W.S., Selsted M.E., Mekalanos J.J. Characterization of defensin resistance phenotypes associated with mutations in the phoP virulence regulon of Salmonella typhimurium. Infect Immun. 58:1990;3706-3710.
    • (1990) Infect Immun , vol.58 , pp. 3706-3710
    • Miller, S.I.1    Pulkkinen, W.S.2    Selsted, M.E.3    Mekalanos, J.J.4
  • 64
    • 0031213832 scopus 로고    scopus 로고
    • The human β-defensin-1 and α-defensins are encoded by adjacent genes: Two peptide families with differing distilfide topology share a common ancestry
    • Liu L, Zhao Z, Heng HHQ, Ganz T. The human β-defensin-1 and α-defensins are encoded by adjacent genes: Two peptide families with differing distilfide topology share a common ancestry. Genomics 1997;43:316-20.
    • (1997) Genomics , vol.43 , pp. 316-320
    • Liu, L.1    Zhao, Z.2    Heng, H.H.Q.3    Ganz, T.4
  • 65
    • 0029900207 scopus 로고    scopus 로고
    • Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells
    • Diamond G., Russell J.P., Bevins C.L. Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells. Proc Natl Acad Sci USA. 93:1996;5156-5160.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5156-5160
    • Diamond, G.1    Russell, J.P.2    Bevins, C.L.3
  • 66
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F., Roumestand C., Gilquin B., Menez A., Toma F. Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins. Science. 254:1991;1521-1523.
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 67
    • 0026590966 scopus 로고
    • I κ B γ, a 70 kd protein identical to the C-terminal half pf p11O NF-κ B: A new member of the I κ B family
    • Inouye J., Kerr L.D., Kakizuka A., Verma I.M. I κ B γ, a 70 kd protein identical to the C-terminal half pf p11O NF-κ B: A new member of the I κ B family. Cell. 68:1992;1109-1120.
    • (1992) Cell , vol.68 , pp. 1109-1120
    • Inouye, J.1    Kerr, L.D.2    Kakizuka, A.3    Verma, I.M.4
  • 68
    • 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.L., 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.L.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 69
    • 0025167968 scopus 로고
    • Primary structures and functions of anti-lipopolysaccharide factor and tachyplesin peptide found in horseshoe crab hemocytes
    • Muta T., Nakamura T., Furunaka H. et al. Primary structures and functions of anti-lipopolysaccharide factor and tachyplesin peptide found in horseshoe crab hemocytes. Adv Exp Med Biol. 256:1990;273-285.
    • (1990) Adv Exp Med Biol , vol.256 , pp. 273-285
    • Muta, T.1    Nakamura, T.2    Furunaka, H.3
  • 70
    • 0025308541 scopus 로고
    • Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): Identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor
    • Muta T., Fujimoto T., Nakajima H., Iwanaga S. Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): Identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. J Biochem. 108:1990;261-266.
    • (1990) J Biochem , vol.108 , pp. 261-266
    • Muta, T.1    Fujimoto, T.2    Nakajima, H.3    Iwanaga, S.4
  • 71
    • 0026677582 scopus 로고
    • Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices
    • Park N.G., Lee S., Oishi O. et al. Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices. Biochemistry. 31:1992;12241-12247.
    • (1992) Biochemistry , vol.31 , pp. 12241-12247
    • Park, N.G.1    Lee, S.2    Oishi, O.3
  • 73
    • 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
  • 74
    • 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. 364:1994;285-288.
    • (1994) FEBS Lett , vol.364 , pp. 285-288
    • Zhao, C.1    Liu, L.2    Lehrer, R.I.3
  • 75
    • 0029295070 scopus 로고
    • Determination of disulphide bridges in PG-2, an antimicrobial peptide from porcine leukocytes
    • Harwig S.S.L., Swiderek K.M., Lee T.D., Lehrer R.I. Determination of disulphide bridges in PG-2, an antimicrobial peptide from porcine leukocytes. J Peptide Sci. 3:1995;207-215.
    • (1995) J Peptide Sci , vol.3 , pp. 207-215
    • Harwig, S.S.L.1    Swiderek, K.M.2    Lee, T.D.3    Lehrer, R.I.4
  • 76
    • 0024349857 scopus 로고
    • Primary structure of a new cysteine proteinase inhibitor from pig leucocytes
    • Ritonja A., Kopitar M., Jerala R., Turk V. Primary structure of a new cysteine proteinase inhibitor from pig leucocytes. FEBS Lett. 255:1989;211-214.
    • (1989) FEBS Lett , vol.255 , pp. 211-214
    • Ritonja, A.1    Kopitar, M.2    Jerala, R.3    Turk, V.4
  • 77
    • 0027528409 scopus 로고
    • Chemotactic and protease-inhibiting activities of antibiotic peptide precursors
    • Verbanac D., Zanetti M., Romeo D. Chemotactic and protease-inhibiting activities of antibiotic peptide precursors. FEBS Lett. 317:1993;255-258.
    • (1993) FEBS Lett , vol.317 , pp. 255-258
    • Verbanac, D.1    Zanetti, M.2    Romeo, D.3
  • 79
    • 0029040564 scopus 로고
    • Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity
    • Tamamura H., Murakami T., Horiuchi S. et al. Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity. Chem Pharm Bull. 43:1995;853-858.
    • (1995) Chem Pharm Bull , vol.43 , pp. 853-858
    • Tamamura, H.1    Murakami, T.2    Horiuchi, S.3
  • 80
    • 0031203411 scopus 로고    scopus 로고
    • Sensitivity of periodontal pathogens to the bactericidal activity of synthetic protegrins, antibiotic peptides derived from porcine leukocytes
    • Miyasaki K.T., Iofel R., Lehrer R.I. Sensitivity of periodontal pathogens to the bactericidal activity of synthetic protegrins, antibiotic peptides derived from porcine leukocytes. J Dent Res. 76:1997;1453-1459.
    • (1997) J Dent Res , vol.76 , pp. 1453-1459
    • Miyasaki, K.T.1    Iofel, R.2    Lehrer, R.I.3
  • 81
    • 0002166857 scopus 로고    scopus 로고
    • Bactenecins: Potent peptide antibiotics for Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans
    • Raj P.A., Edgerton G., Edgerton M. Bactenecins: Potent peptide antibiotics for Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans. Int J Oral Biol. 22:1997;73-80.
    • (1997) Int J Oral Biol , vol.22 , pp. 73-80
    • Raj, P.A.1    Edgerton, G.2    Edgerton, M.3


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