메뉴 건너뛰기




Volumn 10, Issue 12, 2015, Pages

Comparative evaluation of the antimicrobial activity of different antimicrobial peptides against a range of pathogenic Bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLARGINYLTRYPTOPHYLLYSYLISOLEUCYLVALYLVALYLISOLEUCYLARGINYLTRYPTOPHYLARGINYLARGININE; ARGINYLLEUCYLALANYLARGINYLISOLEUCYLVALYLVALYLISOLEUCYLARGINYLVALYLALANYLARGININE; GLYCYLASPARAGINYLASPARAGINYLARGINYLPROLYLVALYLTYROSYLISOLEUCYLPROLYLGLUTAMINYLPROLYLARGINYLPROLYLPROLYLHISTIDINYLPROLYLARGINYLISOLEUCINE; GLYCYLISOLEUCYLHISTIDINYLASPARTYLISOLEUCYLLEUCYLLYSYLTYROSYLGLYCYLLYSYLPROLYLSERINE; INDOLICIDIN; LIPOPOLYSACCHARIDE; LYSYLLEUCYLARGINYLLYSYLLEUCYLPHENYLALANYLARGINYLLYSYLLEUCYLLEUCYLLYSYLLEUCYLISOLEUCYLARGINYLLYSYLLEUCYLLEUCYLARGININE; LYSYLTRYPTOPHYLLYSYLVALYLPHENYLALANYLLYSYLLYSYLISOLEUCYLGLUTAMYLLYSYLMETHIONYLGLYCYLARGINYLASPARAGINYLISOLEUCYLARGINYLASPARAGINYLGLYCYLISOLEUCYLVALYLLYSYLALANYLGLYCYLPROLYLALANYLISOLEUCYLALANYLVALYLLEUCYLGLYCYLGLUTAMYLALANYLLYSYLALANYLLEUCYLGLYCINE; MELITTIN; POLYPEPTIDE ANTIBIOTIC AGENT; SERYLTRYPTOPHYLLEUCYLSERYLLYSYLTHREONYLALANYLLYSYLLYSYLLEUCYLGLUTAMYLASPARAGINYLSERYLALANYLLYSYLLYSYLARGINYLISOLEUCYLSERYLGLUTAMYLGLCYLISOLEUCYLALANYLISOLEUCYLALANYLISOLEUCYLGLUTAMINYLGLYCYLGLYCYLPROLYLARGININE; UNCLASSIFIED DRUG; VALYLASPARTYLLYSYLGLYCYLSERYLTYROSYLLEUCYLPROLYLARGINYLPROLYLTHREONYLPROLYLPROLYLARGINYLPROLYLISOLEUCYLTYROSYLASPARAGINYLARGINYLASPARAGINE; VALYLASPARTYLLYSYLPROLYLASPARTYLTYROSYLARGINYLPROLYLARGINYLPROLYLARGINYLPROLYLPROLYLASPARAGINYLMETHIONINE; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; PEPTIDE HYDROLASE;

EID: 84957108704     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0144611     Document Type: Article
Times cited : (158)

References (66)
  • 1
    • 55249118635 scopus 로고    scopus 로고
    • Resistance in bacteria of the food chain: Epidemiology and control strategies
    • Aarestrup FM, Wegener HC, Collignon P. Resistance in bacteria of the food chain: epidemiology and control strategies. Expert Rev Anti Infect Ther. 2008; 6: 733-750. doi: 10.1586/14787210.6.5.733
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 733-750
    • Aarestrup, F.M.1    Wegener, H.C.2    Collignon, P.3
  • 2
    • 66949137742 scopus 로고    scopus 로고
    • World Health Organization ranking of antimicrobials according to their importance in human medicine: A critical step for developing risk management strategies for the use of antimicrobials in food production animals
    • Collignon P, Powers JH, Chiller TM, Aidara-Kane A, Aarestrup FM. World Health Organization ranking of antimicrobials according to their importance in human medicine: A critical step for developing risk management strategies for the use of antimicrobials in food production animals. Clin Infect Dis. 2009; 49: 132-141. doi: 10.1086/599374
    • (2009) Clin Infect Dis , vol.49 , pp. 132-141
    • Collignon, P.1    Powers, J.H.2    Chiller, T.M.3    Aidara-Kane, A.4    Aarestrup, F.M.5
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 2002; 415: 389-395. doi: 10.1038/415389a
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 79955164524 scopus 로고    scopus 로고
    • Natural roles of antimicrobial peptides in microbes, plants and animals
    • Maróti G, Kereszt A, Kondorosi E, Mergaert P. Natural roles of antimicrobial peptides in microbes, plants and animals. Res Microbiol. 2011; 162: 363-374. doi: 10.1016/j.resmic.2011.02.005
    • (2011) Res Microbiol , vol.162 , pp. 363-374
    • Maróti, G.1    Kereszt, A.2    Kondorosi, E.3    Mergaert, P.4
  • 5
    • 33646532402 scopus 로고    scopus 로고
    • Host defence peptides from invertebrates-emerging antimicrobial strategies
    • Hancock REW, Brown KL, Mookherjee N. Host defence peptides from invertebrates-emerging antimicrobial strategies. Immunobiology. 2006; 211: 315-322. doi: 10.1016/j.imbio.2005.10.017
    • (2006) Immunobiology , vol.211 , pp. 315-322
    • Rew, H.1    Brown, K.L.2    Mookherjee, N.3
  • 6
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock REW, Lehrer R. Cationic peptides: A new source of antibiotics. Trends in Biotechnology. 1998. pp. 82-88. doi: 10.1016/S0167-7799(97)01156-6
    • (1998) Trends in Biotechnology , pp. 82-88
    • Rew, H.1    Lehrer, R.2
  • 8
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol. 2005; 3: 238-250. doi: 10.1038/nrmicro1098
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 9
    • 77955096108 scopus 로고    scopus 로고
    • A 90-day oral toxicity study of nisin A an anti-microbial peptide derived from Lactococcus lactis subsp lactis in F344 rats
    • Hagiwara A, Imai N, Nakashima H, Toda Y, Kawabe M, Furukawa F, et al. A 90-day oral toxicity study of nisin A, an anti-microbial peptide derived from Lactococcus lactis subsp. lactis, in F344 rats. Food Chem Toxicol. Elsevier Ltd; 2010; 48: 2421-2428. doi: 10.1016/j.fct.2010.06.002
    • (2011) Food Chem Toxicol Elsevier Ltd , vol.48 , pp. 2421-2428
    • Hagiwara, A.1    Imai, N.2    Nakashima, H.3    Toda, Y.4    Kawabe, M.5    Furukawa, F.6
  • 11
    • 34247098941 scopus 로고    scopus 로고
    • Antibiotic properties and applications of lactoferrin
    • Weinberg ED. Antibiotic properties and applications of lactoferrin. Curr Pharm Des. 2007; 13: 801-811. doi: 10.2174/138161207780363095
    • (2007) Curr Pharm des , vol.13 , pp. 801-811
    • Weinberg, E.D.1
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A. 2000; 97: 6640-6645. doi: 10.1073/pnas.120163297
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol Syst Biol. 2006; 2: 2006.0008. doi: 10. 1038/msb4100050
    • (2006) Mol Syst Biol , vol.2 , Issue.2006 , pp. 0008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 14
    • 0032705847 scopus 로고    scopus 로고
    • Production of viable cultures of Flavobacterium psychrophilum: Approach and control
    • Michel C, Antonio D, Hedrick RP. Production of viable cultures of Flavobacterium psychrophilum: Approach and control. Res Microbiol. 1999; 150: 351-358. Available: http://www.ncbi.nlm.nih.gov/pubmed/10422696.
    • (1999) Res Microbiol , vol.150 , pp. 351-358
    • Michel, C.1    Antonio, D.2    Hedrick, R.P.3
  • 16
    • 0015527253 scopus 로고
    • Habermann E. Bee and Wasp Venoms. Sci. 1972; 177: 314-322. doi: 10.1126/science.177.4046.314
    • (1972) Wasp Venoms Sci , vol.177 , pp. 314-322
    • Habermann, E.B.1
  • 18
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • Casteels P, Ampe C, Jacobs F, Vaeck M, Tempst P. Apidaecins: Antibacterial peptides from honeybees. EMBO J. 1989; 8: 2387-2391.
    • (1989) EMBO J , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 19
    • 0001924808 scopus 로고    scopus 로고
    • The inducible antibacterial peptides of the Hemipteran insect Palomena prasina: Identification of a unique family of prolinerich peptides and of a novel insect defensin
    • Chernysh S, Cociancich S, Briand J-P, Hetru C, Bulet P. The inducible antibacterial peptides of the Hemipteran insect Palomena prasina: Identification of a unique family of prolinerich peptides and of a novel insect defensin. Journal of Insect Physiology. 1996. pp. 81-89. doi: 10.1016/0022-1910(95) 00085-2
    • (1996) Journal of Insect Physiology , pp. 81-89
    • Chernysh, S.1    Cociancich, S.2    Briand, J.-P.3    Hetru, C.4    Bulet, P.5
  • 20
    • 0036953281 scopus 로고    scopus 로고
    • Development of novel antibacterial peptides that kill resistant isolates
    • Cudic M, Condie B a, Weiner DJ, Lysenko ES, Xiang ZQ, Insug O, et al. Development of novel antibacterial peptides that kill resistant isolates. Peptides. 2002; 23: 2071-2083. Available: http://www.ncbi. nlm.nih.gov/pubmed/12535685.
    • (2002) Peptides , vol.23 , pp. 2071-2083
    • Cudic, M.1    Condie, B.A.2    Weiner, D.J.3    Lysenko, E.S.4    Xiang, Z.Q.5    Insug, O.6
  • 21
    • 67649424250 scopus 로고    scopus 로고
    • Augmentation of the antimicrobial activities of Guinea pig cathelicidin CAP11-derived peptides by amino acid substitutions
    • Okuda D, Yomogida S, Kuwahara-Arai K. Augmentation of the antimicrobial activities of guinea pig cathelicidin CAP11-derived peptides by amino acid substitutions. Int J Mol Med. 2009; 501-508. doi: 10.3892/ijmm
    • (2009) Int J Mol Med , pp. 501-508
    • Okuda, D.1    Yomogida, S.2    Kuwahara-Arai, K.3
  • 22
    • 0035884820 scopus 로고    scopus 로고
    • Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-Alpha by blocking the binding of LPS to CD14(+) cells
    • Nagaoka I, Hirota S, Niyonsaba F, Hirata M, Adachi Y, Tamura H, et al. Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-Alpha by blocking the binding of LPS to CD14(+) cells. J Immunol. 2001; 167: 3329-3338.
    • (2001) J Immunol , vol.167 , pp. 3329-3338
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3    Hirata, M.4    Adachi, Y.5    Tamura, H.6
  • 24
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla TJ, Nedra Karunaratne D, Hancock REW. Mode of action of the antimicrobial peptide indolicidin. J Biol Chem. 1996; 271: 19298-19303. doi: 10.1074/jbc.271.32.19298
    • (1996) J Biol Chem , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Nedra Karunaratne, D.2    Rew, H.3
  • 25
    • 36849010657 scopus 로고    scopus 로고
    • Structural and thermodynamic analyses of the interaction between melittin and lipopolysaccharide
    • Bhunia A, Domadia PN, Bhattacharjya S. Structural and thermodynamic analyses of the interaction between melittin and lipopolysaccharide. Biochim Biophys Acta-Biomembr. 2007; 1768: 3282-3291. doi: 10.1016/j.bbamem.2007.07.017
    • (2007) Biochim Biophys Acta-Biomembr , vol.1768 , pp. 3282-3291
    • Bhunia, A.1    Domadia, P.N.2    Bhattacharjya, S.3
  • 26
    • 0035007963 scopus 로고    scopus 로고
    • Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids
    • Gutsmann T, Hagge SO, Larrick JW, Seydel U, Wiese a. Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids. Biophys J. Elsevier; 2001; 80: 2935-2945. doi: 10.1016/S0006-3495(01)76259-5
    • (2001) Biophys J Elsevier , vol.80 , pp. 2935-2945
    • Gutsmann, T.1    Hagge, S.O.2    Larrick, J.W.3    Seydel, U.4    Wiese, A.5
  • 29
    • 0033995146 scopus 로고    scopus 로고
    • Synergistic actions of antibacterial neutrophil defensins and cathelicidins
    • Nagaoka I, Hirota S, Yomogida S, Ohwada A, Hirata M. Synergistic actions of antibacterial neutrophil defensins and cathelicidins. Inflamm Res. 2000; 49: 73-79. doi: 10.1007/s000110050561
    • (2000) Inflamm Res , vol.49 , pp. 73-79
    • Nagaoka, I.1    Hirota, S.2    Yomogida, S.3    Ohwada, A.4    Hirata, M.5
  • 31
    • 0029977691 scopus 로고    scopus 로고
    • Purification of the 11-And 5-kDa antibacterial polypeptides from Guinea pig neutrophils
    • Yomogida S, Nagaoka I, Yamashita T. Purification of the 11-And 5-kDa antibacterial polypeptides from guinea pig neutrophils. Arch Biochem Biophys. 1996; 328: 219-226. doi: 10.1006/abbi.1996.0166
    • (1996) Arch Biochem Biophys , vol.328 , pp. 219-226
    • Yomogida, S.1    Nagaoka, I.2    Yamashita, T.3
  • 32
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect Immun. 1993; 61: 2978-84. Available: http://www.ncbi.nlm.nih.gov/pubmed/8514403.
    • (1993) Infect Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 34
    • 0024331982 scopus 로고
    • Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin
    • Lee JY, Boman A, Sun CX, Andersson M, Jörnvall H, Mutt V, et al. Antibacterial peptides from pig intestine: isolation of a mammalian cecropin. Proc Natl Acad Sci U S A. 1989; 86: 9159-62. Available: http://www.ncbi.nlm.nih.gov/pubmed/2512577.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 9159-9162
    • Lee, J.Y.1    Boman, A.2    Sun, C.X.3    Andersson, M.4    Jörnvall, H.5    Mutt, V.6
  • 36
    • 23444451770 scopus 로고    scopus 로고
    • High-Throughput generation of small antibacterial peptides with improved activity
    • Hilpert K, Volkmer-Engert R, Walter T, Hancock REW. High-Throughput generation of small antibacterial peptides with improved activity. Nat Biotechnol. 2005; 23: 1008-1012. doi: 10.1038/nbt1113
    • (2005) Nat Biotechnol , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 37
    • 0032907969 scopus 로고    scopus 로고
    • Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide
    • Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob Agents Chemother. 1999; 43: 1274-6. Available: http://www.ncbi.nlm.nih.gov/pubmed/10223951.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1274-1276
    • Wu, M.1    Hancock, R.E.2
  • 38
    • 70449523332 scopus 로고    scopus 로고
    • Myxinidin, a novel antimicrobial peptide from the epidermal mucus of hagfish, Myxine glutinosa L
    • Subramanian S, Ross NW, MacKinnon SL. Myxinidin, a novel antimicrobial peptide from the epidermal mucus of hagfish, Myxine glutinosa L. Mar Biotechnol (NY). 2009; 11: 748-757. doi: 10.1007/s10126-009-9189-y
    • (2009) Mar Biotechnol (NY) , vol.11 , pp. 748-757
    • Subramanian, S.1    Ross, N.W.2    MacKinnon, S.L.3
  • 39
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus
    • Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru C, et al. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus. Biochem J. 1994; 300 (Pt 2: 567-575.
    • (1994) Biochem J , vol.300 , pp. 567-575
    • Cociancich, S.1    Dupont, A.2    Hegy, G.3    Lanot, R.4    Holder, F.5    Hetru, C.6
  • 40
    • 84883409216 scopus 로고    scopus 로고
    • Process of inducing pores in membranes by melittin
    • Lee M-T, Sun T-L, Hung W-C, Huang HW. Process of inducing pores in membranes by melittin. Proc Natl Acad Sci U S A. 2013; 110: 14243-14248. doi: 10.1073/pnas.1307010110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14243-14248
    • Lee, M.-T.1    Sun, T.-L.2    Hung, W.-C.3    Huang, H.W.4
  • 41
    • 76049129382 scopus 로고    scopus 로고
    • Structure-guided de novo design of a-helical antimicrobial peptide with enhanced specificity
    • Huang JF, Xu YM, Hao DM, Huang YB, Liu Y, Chen YX. Structure-guided de novo design of a-helical antimicrobial peptide with enhanced specificity. Pure Appl Chem. 2010; 82: 243-257. doi: 10.1351/paccon-09-01-12
    • (2011) Pure Appl Chem , vol.82 , pp. 243-257
    • Huang, J.F.1    Xu, Y.M.2    Hao, D.M.3    Huang, Y.B.4    Liu, Y.5    Chen, Y.X.6
  • 42
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides
    • Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. Antimicrob Agents Chemother. 2007; 51: 1398-1406. doi: 10.1128/AAC.00925-06
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1398-1406
    • Chen, Y.1    Guarnieri, M.T.2    Vasil, A.I.3    Vasil, M.L.4    Mant, C.T.5    Hodges, R.S.6
  • 43
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides
    • Jiang Z, Vasil AI, Hale JD, Hancock REW, Vasil ML, Hodges RS. Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides. Biopolymers. 2008; 90: 369-383. doi: 10.1002/bip.20911
    • (2008) Biopolymers , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Rew, H.4    Vasil, M.L.5    Hodges, R.S.6
  • 44
    • 84925884356 scopus 로고    scopus 로고
    • Role of helicity of α-helical antimicrobial peptides to improve specificity
    • Huang Y, He L, Li G, Zhai N, Jiang H, Chen Y. Role of helicity of α-helical antimicrobial peptides to improve specificity. Protein Cell. 2014; 5: 631-642. doi: 10.1007/s13238-014-0061-0
    • (2014) Protein Cell , vol.5 , pp. 631-642
    • Huang, Y.1    He, L.2    Li, G.3    Zhai, N.4    Jiang, H.5    Chen, Y.6
  • 45
    • 77956125592 scopus 로고    scopus 로고
    • Easy strategy to protect antimicrobial peptides from fast degradation in serum
    • Knappe D, Henklein P, Hoffmann R, Hilpert K. Easy strategy to protect antimicrobial peptides from fast degradation in serum. Antimicrob Agents Chemother. 2010; 54: 4003-4005. doi: 10.1128/AAC.00300-10
    • (2011) Antimicrob Agents Chemother , vol.54 , pp. 4003-4005
    • Knappe, D.1    Henklein, P.2    Hoffmann, R.3    Hilpert, K.4
  • 46
    • 79551517588 scopus 로고    scopus 로고
    • Highly selective end-Tagged antimicrobial peptides derived from PRELP
    • Neyrolles O, editor
    • Malmsten M, Kasetty G, Pasupuleti M, Alenfall J, Schmidtchen A. Highly Selective End-Tagged Antimicrobial Peptides Derived from PRELP. Neyrolles O, editor. PLoS One. 2011; 6: e16400. doi: 10.1371/journal.pone.0016400
    • (2011) PLoS One , vol.6 , pp. e16400
    • Malmsten, M.1    Kasetty, G.2    Pasupuleti, M.3    Alenfall, J.4    Schmidtchen, A.5
  • 47
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37
    • Strömstedt AA, Pasupuleti M, Schmidtchen A, Malmsten M. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob Agents Chemother. 2009; 53: 593-602. doi: 10.1128/AAC.00477-08
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 593-602
    • Strömstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 48
    • 79960950287 scopus 로고    scopus 로고
    • Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches
    • Giuliani A, Rinaldi AC. Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches. Cellular and Molecular Life Sciences. 2011. pp. 2255-2266. doi: 10.1007/s00018-011-0717-3
    • (2011) Cellular and Molecular Life Sciences , pp. 2255-2266
    • Giuliani, A.1    Rinaldi, A.C.2
  • 49
    • 77956929341 scopus 로고    scopus 로고
    • Scientific opinion of the panel on biological hazards /Microbiological risk assessment in feedingstuffs for food-producing animals
    • EFSA
    • EFSA. Scientific Opinion of the Panel on Biological Hazards /Microbiological risk assessment in feedingstuffs for food-producing animals. EFSA J. 2008; 1-84. Available: http://www.elika.net/datos/articulos/Archivo297/BIOHAZ-PiensosSalmonella08.pdf.
    • (2008) EFSA J , pp. 1-84
  • 50
    • 33745248088 scopus 로고    scopus 로고
    • Optimization of extrusion conditions for elimination of mesophilic bacteria during thermal processing of animal feed mash
    • Okelo PO, Wagner DD, Carr LE, Wheaton FW, Douglass LW, Joseph SW. Optimization of extrusion conditions for elimination of mesophilic bacteria during thermal processing of animal feed mash. Anim Feed Sci Technol. 2006; 129: 116-137. doi: 10.1016/j.anifeedsci.2005.12.011
    • (2006) Anim Feed Sci Technol , vol.129 , pp. 116-137
    • Okelo, P.O.1    Wagner, D.D.2    Carr, L.E.3    Wheaton, F.W.4    Douglass, L.W.5    Joseph, S.W.6
  • 51
    • 82455192696 scopus 로고    scopus 로고
    • Influence of feed processing on the efficacy of exogenous enzymes in broiler diets
    • Amerah AM, Gilbert C, Simmins PH, Ravindran V. Influence of feed processing on the efficacy of exogenous enzymes in broiler diets. Worlds Poult Sci J. 2011; 67: 29-46. doi: 10.1017/S0043933911000031
    • (2011) Worlds Poult Sci J , vol.67 , pp. 29-46
    • Amerah, A.M.1    Gilbert, C.2    Simmins, P.H.3    Ravindran, V.4
  • 52
    • 67650957816 scopus 로고    scopus 로고
    • New strategies for novel antibiotics: Peptides targeting bacterial cell membranes
    • Lohner K. New strategies for novel antibiotics: Peptides targeting bacterial cell membranes. General Physiology and Biophysics. 2009. pp. 105-116. doi: 10.4149/gpb-2009-02-105
    • (2009) General Physiology and Biophysics , pp. 105-116
    • Lohner, K.1
  • 54
    • 0027409501 scopus 로고
    • Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in gram-negative enteric bacteria
    • Vaara M. Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in gram-negative enteric bacteria. Antimicrobial Agents and Chemotherapy. 1993. pp. 354-356. doi: 10. 1128/AAC.37.2.354
    • (1993) Antimicrobial Agents and Chemotherapy , pp. 354-356
    • Vaara, M.1
  • 55
    • 0033037301 scopus 로고    scopus 로고
    • Outer membrane permeability barrier in Escherichia coli mutants that are defective in the late acyltransferases of lipid A biosynthesis
    • Vaara M, Nurminen M. Outer membrane permeability barrier in Escherichia coli mutants that are defective in the late acyltransferases of lipid A biosynthesis. Antimicrob Agents Chemother. 1999; 43: 1459-1462.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1459-1462
    • Vaara, M.1    Nurminen, M.2
  • 57
    • 0033806409 scopus 로고    scopus 로고
    • Mutation of the lipopolysaccharide core glycosyltransferase encoded by waaG destabilizes the outer membrane of Escherichia coli by interfering with core phosphorylation
    • Yethon JA, Vinogradov E, Perry MB, Whitfield C. Mutation of the lipopolysaccharide core glycosyltransferase encoded by waaG destabilizes the outer membrane of Escherichia coli by interfering with core phosphorylation. J Bacteriol. 2000; 182: 5620-5623. doi: 10.1128/JB.182.19.5620-5623.2000
    • (2000) J Bacteriol , vol.182 , pp. 5620-5623
    • Yethon, J.A.1    Vinogradov, E.2    Perry, M.B.3    Whitfield, C.4
  • 58
    • 33745172477 scopus 로고    scopus 로고
    • One group of genetically similar Listeria monocytogenes strains frequently dominates and persists in several fish slaughter-And smokehouses
    • Wulff G, Gram L, Ahrens P, Vogel BF. One group of genetically similar Listeria monocytogenes strains frequently dominates and persists in several fish slaughter-And smokehouses. Appl Environ Microbiol. 2006; 72: 4313-4322. doi: 10.1128/AEM.02288-05
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4313-4322
    • Wulff, G.1    Gram, L.2    Ahrens, P.3    Vogel, B.F.4
  • 59
    • 33745004120 scopus 로고    scopus 로고
    • First description of non-motile Yersinia ruckeri serovar i strains causing disease in rainbow trout, Oncorhynchus mykiss (Walbaum), cultured in Spain
    • Fouz B, Zarza C, Amaro C. First description of non-motile Yersinia ruckeri serovar I strains causing disease in rainbow trout, Oncorhynchus mykiss (Walbaum), cultured in Spain. J Fish Dis. 2006; 29: 339-346. doi: 10.1111/j.1365-2761.2006.00723.x
    • (2006) J Fish Dis , vol.29 , pp. 339-346
    • Fouz, B.1    Zarza, C.2    Amaro, C.3
  • 61
    • 0033773438 scopus 로고    scopus 로고
    • Comparative functional characterization in vitro of heptosyltransferase i (WaaC) and II (WaaF) from Escherichia coli
    • Gronow S, Brabetz W, Brade H. Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli. Eur J Biochem. 2000; 267: 6602-6611. doi: 10.1046/j. 1432-1327.2000.01754.x
    • (2000) Eur J Biochem , vol.267 , pp. 6602-6611
    • Gronow, S.1    Brabetz, W.2    Brade, H.3
  • 62
    • 0345597983 scopus 로고    scopus 로고
    • Efficient chemical synthesis of both anomers of ADP L-glycero-And D-glycero-D-manno-heptopyranose
    • Zamyatina A, Gronow S, Puchberger M, Graziani A, Hofinger A, Kosma P. Efficient chemical synthesis of both anomers of ADP L-glycero-And D-glycero-D-manno-heptopyranose. Carbohydr Res. 2003; 338: 2571-2589. doi: 10.1016/S0008-6215(03)00319-7
    • (2003) Carbohydr Res , vol.338 , pp. 2571-2589
    • Zamyatina, A.1    Gronow, S.2    Puchberger, M.3    Graziani, A.4    Hofinger, A.5    Kosma, P.6
  • 63
    • 0033987369 scopus 로고    scopus 로고
    • The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose
    • Valvano MA, Marolda CL, Bittner M, Glaskin-Clay M, Simon TL, Klena JD. The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose. J Bacteriol. 2000; 182: 488-497. doi: 10.1128/JB.182.2.488-497.2000
    • (2000) J Bacteriol , vol.182 , pp. 488-497
    • Valvano, M.A.1    Marolda, C.L.2    Bittner, M.3    Glaskin-Clay, M.4    Simon, T.L.5    Klena, J.D.6
  • 64
    • 22544462795 scopus 로고    scopus 로고
    • Functional analysis of the glyceromanno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis
    • McArthur F, Andersson CE, Loutet S, Mowbray SL, Valvano MA. Functional analysis of the glyceromanno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis. J Bacteriol. 2005; 187: 5292-5300. doi: 10.1128/JB. 187.15.5292-5300.2005
    • (2005) J Bacteriol , vol.187 , pp. 5292-5300
    • McArthur, F.1    Andersson, C.E.2    Loutet, S.3    Mowbray, S.L.4    Valvano, M.A.5
  • 65
    • 0026751197 scopus 로고
    • Role of the rfaG and rfaP genes in determining the lipopolysaccharide core structure and cell surface properties of Escherichia coli K-12
    • Parker CT, Kloser AW, Schnaitman CA, Stein MA, Gottesman S, Gibson BW. Role of the rfaG and rfaP genes in determining the lipopolysaccharide core structure and cell surface properties of Escherichia coli K-12. J Bacteriol. 1992; 174: 2525-2538.
    • (1992) J Bacteriol , vol.174 , pp. 2525-2538
    • Parker, C.T.1    Kloser, A.W.2    Schnaitman, C.A.3    Stein, M.A.4    Gottesman, S.5    Gibson, B.W.6
  • 66
    • 19244370919 scopus 로고    scopus 로고
    • Structural analysis of oligosaccharides from lipopolysaccharide (LPS) of Escherichia coli K12 Strain W3100 Reveals a Link between Inner and Outer Core LPS Biosynthesis
    • Möller-Loennies S, Lindner B, Brade H. Structural Analysis of Oligosaccharides from Lipopolysaccharide (LPS) of Escherichia coli K12 Strain W3100 Reveals a Link between Inner and Outer Core LPS Biosynthesis. J Biol Chem. 2003; 278: 34090-34101. doi: 10.1074/jbc.M303985200
    • (2003) J Biol Chem , vol.278 , pp. 34090-34101
    • Möller-Loennies, S.1    Lindner, B.2    Brade, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.