메뉴 건너뛰기




Volumn 4, Issue FEB, 2016, Pages

Potentiating the activity of nisin against Escherichia coli

Author keywords

Fusion; Gram negative; Lantibiotic; Nisin; Outer membrane

Indexed keywords


EID: 85010612712     PISSN: None     EISSN: 2296634X     Source Type: Journal    
DOI: 10.3389/fcell.2016.00007     Document Type: Article
Times cited : (59)

References (48)
  • 1
    • 18144369721 scopus 로고    scopus 로고
    • Mode of action of lipid II-targeting lantibiotics
    • Bauer, R., and Dicks, L. M. T. (2005). Mode of action of lipid II-targeting lantibiotics. Int. J. Food Microbiol. 101, 201-216. doi: 10.1016/j.ijfoodmicro.2004.11.007
    • (2005) Int. J. Food Microbiol , vol.101 , pp. 201-216
    • Bauer, R.1    Dicks, L.M.T.2
  • 2
    • 84872048892 scopus 로고    scopus 로고
    • Novel apidaecin 1b analogs with superior serum stabilities for treatment of infections by gram-negative pathogens
    • Berthold, N., Czihal, P., Fritsche, S., Sauer, U., Schiffer, G., Knappe, D., et al. (2013). Novel apidaecin 1b analogs with superior serum stabilities for treatment of infections by gram-negative pathogens. Antimicrob. Agents Chemother. 57, 402-409. doi: 10.1128/AAC.01923-12
    • (2013) Antimicrob. Agents Chemother , vol.57 , pp. 402-409
    • Berthold, N.1    Czihal, P.2    Fritsche, S.3    Sauer, U.4    Schiffer, G.5    Knappe, D.6
  • 4
    • 31544432925 scopus 로고    scopus 로고
    • Novel surface display system for proteins on non-genetically modified gram-positive bacteria
    • Bosma, T., Kanninga, R., Neef, J., Audouy, S. A. L., van Roosmalen, M. L., Steen, A., et al. (2006). Novel surface display system for proteins on non-genetically modified gram-positive bacteria. Appl. Environ. Microbiol. 72, 880-889. doi: 10.1128/AEM.72.1.880-889.2006
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 880-889
    • Bosma, T.1    Kanninga, R.2    Neef, J.3    Audouy, S.A.L.4    van Roosmalen, M.L.5    Steen, A.6
  • 5
    • 0032719376 scopus 로고    scopus 로고
    • Effect of chelators and nisin produced in situ on inhibition and inactivation of Gram negatives
    • Boziaris, I. S., and Adams, M. R. (1999). Effect of chelators and nisin produced in situ on inhibition and inactivation of Gram negatives. Int. J. Food Microbiol. 53, 105-113. doi: 10.1016/S0168-1605(99)00139-7
    • (1999) Int. J. Food Microbiol , vol.53 , pp. 105-113
    • Boziaris, I.S.1    Adams, M.R.2
  • 6
    • 33645474378 scopus 로고    scopus 로고
    • Lipid II as a target for antibiotics
    • Breukink, E., and de Kruijff, B. (2006). Lipid II as a target for antibiotics. Nat. Rev. Drug Discov. 5, 321-332. doi: 10.1038/nrd2004
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 321-332
    • Breukink, E.1    de Kruijff, B.2
  • 8
    • 84921389409 scopus 로고    scopus 로고
    • Effect of divalent cation removal on the structure of gram-negative bacterial outer membrane models
    • Clifton, L. A., Skoda, M. W. A., Le Brun, A. P., Ciesielski, F., Kuzmenko, I., Holt, S. A., et al. (2015). Effect of divalent cation removal on the structure of gram-negative bacterial outer membrane models. Langmuir ACS J. Surf. Colloids 31, 404-412. doi: 10.1021/la504407v
    • (2015) Langmuir ACS J. Surf. Colloids , vol.31 , pp. 404-412
    • Clifton, L.A.1    Skoda, M.W.A.2    Le Brun, A.P.3    Ciesielski, F.4    Kuzmenko, I.5    Holt, S.A.6
  • 9
    • 84864148170 scopus 로고    scopus 로고
    • Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant Gram-negative pathogens
    • Czihal, P., Knappe, D., Fritsche, S., Zahn, M., Berthold, N., Piantavigna, S., et al. (2012). Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant Gram-negative pathogens. ACS Chem. Biol. 7, 1281-1291. doi: 10.1021/cb300063v
    • (2012) ACS Chem. Biol , vol.7 , pp. 1281-1291
    • Czihal, P.1    Knappe, D.2    Fritsche, S.3    Zahn, M.4    Berthold, N.5    Piantavigna, S.6
  • 10
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter, P. G., Kuipers, O. P., and de Vos, W. M. (1996). Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62, 3662-3667
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3662-3667
    • de Ruyter, P.G.1    Kuipers, O.P.2    de Vos, W.M.3
  • 12
    • 0036629937 scopus 로고    scopus 로고
    • Structure and function of lipopolysaccharides
    • Erridge, C., Bennett-Guerrero, E., and Poxton, I. R. (2002). Structure and function of lipopolysaccharides. Microbes Infect. 4, 837-851. doi: 10.1016/S1286-4579(02)01604-0
    • (2002) Microbes Infect , vol.4 , pp. 837-851
    • Erridge, C.1    Bennett-Guerrero, E.2    Poxton, I.R.3
  • 13
    • 84867326984 scopus 로고    scopus 로고
    • Bioengineered nisin A derivatives with enhanced activity against both Gram positive and Gram negative pathogens
    • Field, D., Begley, M., O'Connor, P. M., Daly, K. M., Hugenholtz, F., Cotter, P. D., et al. (2012). Bioengineered nisin A derivatives with enhanced activity against both Gram positive and Gram negative pathogens. PLoS ONE 7:e46884. doi: 10.1371/journal.pone.0046884
    • (2012) PLoS ONE , vol.7
    • Field, D.1    Begley, M.2    O'Connor, P.M.3    Daly, K.M.4    Hugenholtz, F.5    Cotter, P.D.6
  • 14
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. (1983). Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154, 1-9
    • (1983) J. Bacteriol , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 15
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper, H. E., Kramer, N. E., Smith, J. L., Hillman, J. D., Zachariah, C., Kuipers, O. P., et al. (2006). An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313, 1636-1637. doi: 10.1126/science.1129818
    • (2006) Science , vol.313 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6
  • 16
    • 0034715173 scopus 로고    scopus 로고
    • Permeability barrier of the Gram-negative bacterial outer membrane with special reference to nisin
    • Helander, I. M., and Mattila-Sandholm, T. (2000). Permeability barrier of the Gram-negative bacterial outer membrane with special reference to nisin. Int. J. Food Microbiol. 60, 153-161. doi: 10.1016/S0168-1605(00)00307-X
    • (2000) Int. J. Food Microbiol , vol.60 , pp. 153-161
    • Helander, I.M.1    Mattila-Sandholm, T.2
  • 17
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert, K., Volkmer-Engert, R., Walter, T., and Hancock, R. E. W. (2005). High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 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
  • 18
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by electroporation
    • Holo, H., and Nes, I. F. (1995). Transformation of Lactococcus by electroporation. Methods Mol. Biol. 47, 195-199. doi: 10.1385/0-89603-310-4:195
    • (1995) Methods Mol. Biol , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 19
    • 4744345463 scopus 로고    scopus 로고
    • The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics
    • Hsu, S.-T. D., Breukink, E., Tischenko, E., Lutters, M. A. G., de Kruijff, B., Kaptein, R., et al. (2004). The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat. Struct. Mol. Biol. 11, 963-967. doi: 10.1038/nsmb830
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 963-967
    • Hsu, S.-T.D.1    Breukink, E.2    Tischenko, E.3    Lutters, M.A.G.4    de Kruijff, B.5    Kaptein, R.6
  • 20
    • 84872106766 scopus 로고    scopus 로고
    • Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences
    • Iliæ, N., Novkoviæ, M., Guida, F., Xhindoli, D., Benincasa, M., Tossi, A., et al. (2013). Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. Biochim. Biophys. Acta 1828, 1004-1012. doi: 10.1016/j.bbamem.2012.11.017
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1004-1012
    • Iliæ, N.1    Novkoviæ, M.2    Guida, F.3    Xhindoli, D.4    Benincasa, M.5    Tossi, A.6
  • 21
    • 25444499680 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin
    • Kluskens, L. D., Kuipers, A., Rink, R., de Boef, E., Fekken, S., Driessen, A. J. M., et al. (2005). Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin. Biochemistry 44, 12827-12834. doi: 10.1021/bi050805p
    • (2005) Biochemistry , vol.44 , pp. 12827-12834
    • Kluskens, L.D.1    Kuipers, A.2    Rink, R.3    de Boef, E.4    Fekken, S.5    Driessen, A.J.M.6
  • 22
    • 77954725852 scopus 로고    scopus 로고
    • Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens
    • Knappe, D., Piantavigna, S., Hansen, A., Mechler, A., Binas, A., Nolte, O., et al. (2010). Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens. J. Med. Chem. 53, 5240-5247. doi: 10.1021/jm100378b
    • (2010) J. Med. Chem , vol.53 , pp. 5240-5247
    • Knappe, D.1    Piantavigna, S.2    Hansen, A.3    Mechler, A.4    Binas, A.5    Nolte, O.6
  • 23
    • 0036855378 scopus 로고    scopus 로고
    • NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin
    • Koponen, O., Tolonen, M., Qiao, M., Wahlström, G., Helin, J., and Saris, P. E. J. (2002). NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin. Microbiol. Read. Engl. 148, 3561-3568. doi: 10.1099/00221287-148-11-3561
    • (2002) Microbiol. Read. Engl , vol.148 , pp. 3561-3568
    • Koponen, O.1    Tolonen, M.2    Qiao, M.3    Wahlström, G.4    Helin, J.5    Saris, P.E.J.6
  • 24
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers, A., de Boef, E., Rink, R., Fekken, S., Kluskens, L. D., Driessen, A. J. M., et al. (2004). NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides. J. Biol. Chem. 279, 22176-22182. doi: 10.1074/jbc.M312789200
    • (2004) J. Biol. Chem , vol.279 , pp. 22176-22182
    • Kuipers, A.1    de Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.M.6
  • 25
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers, O. P., Beerthuyzen, M. M., Siezen, R. J., and de Vos, W. M. (1993). Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. Eur. J. Biochem. 216, 281-291
    • (1993) Eur. J. Biochem , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    de Vos, W.M.4
  • 26
    • 0030888910 scopus 로고    scopus 로고
    • Controlled overproduction of proteins by lactic acid bacteria
    • Kuipers, O. P., de Ruyter, P. G., Kleerebezem, M., and de Vos, W. M. (1997). Controlled overproduction of proteins by lactic acid bacteria. Trends Biotechnol. 15, 135-140. doi: 10.1016/S0167-7799(97)01029-9
    • (1997) Trends Biotechnol , vol.15 , pp. 135-140
    • Kuipers, O.P.1    de Ruyter, P.G.2    Kleerebezem, M.3    de Vos, W.M.4
  • 27
    • 33746910238 scopus 로고    scopus 로고
    • Apidaecin-type peptides: biodiversity, structure-function relationships and mode of action
    • Li, W.-F., Ma, G.-X., and Zhou, X.-X. (2006). Apidaecin-type peptides: biodiversity, structure-function relationships and mode of action. Peptides 27, 2350-2359. doi: 10.1016/j.peptides.2006.03.016
    • (2006) Peptides , vol.27 , pp. 2350-2359
    • Li, W.-F.1    Ma, G.-X.2    Zhou, X.-X.3
  • 28
    • 0025317783 scopus 로고
    • The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
    • Lipinska, B., Zylicz, M., and Georgopoulos, C. (1990). The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172, 1791-1797
    • (1990) J. Bacteriol , vol.172 , pp. 1791-1797
    • Lipinska, B.1    Zylicz, M.2    Georgopoulos, C.3
  • 29
    • 38949166717 scopus 로고    scopus 로고
    • Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin
    • Lubelski, J., Rink, R., Khusainov, R., Moll, G. N., and Kuipers, O. P. (2008). Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin. Cell. Mol. Life Sci. 65, 455-476. doi: 10.1007/s00018-007-7171-2
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 455-476
    • Lubelski, J.1    Rink, R.2    Khusainov, R.3    Moll, G.N.4    Kuipers, O.P.5
  • 30
    • 77950113113 scopus 로고    scopus 로고
    • Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the Class I nisin synthetic machinery and leader sequence
    • Majchrzykiewicz, J. A., Lubelski, J., Moll, G. N., Kuipers, A., Bijlsma, J. J. E., Kuipers, O. P., et al. (2010). Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the Class I nisin synthetic machinery and leader sequence. Antimicrob. Agents Chemother. 54, 1498-1505. doi: 10.1128/AAC.00883-09
    • (2010) Antimicrob. Agents Chemother , vol.54 , pp. 1498-1505
    • Majchrzykiewicz, J.A.1    Lubelski, J.2    Moll, G.N.3    Kuipers, A.4    Bijlsma, J.J.E.5    Kuipers, O.P.6
  • 31
  • 32
    • 84877865975 scopus 로고    scopus 로고
    • Synergistic effect between colistin and bacteriocins in controlling Gram-negative pathogens and their potential to reduce antibiotic toxicity in mammalian epithelial cells
    • Naghmouchi, K., Baah, J., Hober, D., Jouy, E., Rubrecht, C., Sané, F., et al. (2013). Synergistic effect between colistin and bacteriocins in controlling Gram-negative pathogens and their potential to reduce antibiotic toxicity in mammalian epithelial cells. Antimicrob. Agents Chemother. 57, 2719-2725. doi: 10.1128/AAC.02328-12
    • (2013) Antimicrob. Agents Chemother , vol.57 , pp. 2719-2725
    • Naghmouchi, K.1    Baah, J.2    Hober, D.3    Jouy, E.4    Rubrecht, C.5    Sané, F.6
  • 33
    • 84925460979 scopus 로고    scopus 로고
    • Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
    • Ortega, M. A., Hao, Y., Zhang, Q., Walker, M. C., van der Donk, W. A., and Nair, S. K. (2015). Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB. Nature 517, 509-512. doi: 10.1038/nature13888
    • (2015) Nature , vol.517 , pp. 509-512
    • Ortega, M.A.1    Hao, Y.2    Zhang, Q.3    Walker, M.C.4    van der Donk, W.A.5    Nair, S.K.6
  • 34
    • 84878574659 scopus 로고    scopus 로고
    • Mechanistic aspects of lanthipeptide leaders
    • Plat, A., Kuipers, A., Rink, R., and Moll, G. N. (2013). Mechanistic aspects of lanthipeptide leaders. Curr. Protein Pept. Sci. 14, 85-96. doi: 10.2174/1389203711314020001
    • (2013) Curr. Protein Pept. Sci , vol.14 , pp. 85-96
    • Plat, A.1    Kuipers, A.2    Rink, R.3    Moll, G.N.4
  • 35
    • 36048994654 scopus 로고    scopus 로고
    • NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides
    • Rink, R., Kluskens, L. D., Kuipers, A., Driessen, A. J. M., Kuipers, O. P., and Moll, G. N. (2007a). NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides. Biochemistry 46, 13179-13189. doi: 10.1021/bi700106z
    • (2007) Biochemistry , vol.46 , pp. 13179-13189
    • Rink, R.1    Kluskens, L.D.2    Kuipers, A.3    Driessen, A.J.M.4    Kuipers, O.P.5    Moll, G.N.6
  • 36
    • 20544436705 scopus 로고    scopus 로고
    • Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes
    • Rink, R., Kuipers, A., de Boef, E., Leenhouts, K. J., Driessen, A. J. M., Moll, G. N., et al. (2005). Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes. Biochemistry 44, 8873-8882. doi: 10.1021/bi050081h
    • (2005) Biochemistry , vol.44 , pp. 8873-8882
    • Rink, R.1    Kuipers, A.2    de Boef, E.3    Leenhouts, K.J.4    Driessen, A.J.M.5    Moll, G.N.6
  • 37
    • 34648825064 scopus 로고    scopus 로고
    • Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation
    • Rink, R., Wierenga, J., Kuipers, A., Kluskens, L. D., Driessen, A. J. M., Kuipers, O. P., et al. (2007b). Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation. Appl. Environ. Microbiol. 73, 5809-5816. doi: 10.1128/AEM.01104-07
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 5809-5816
    • Rink, R.1    Wierenga, J.2    Kuipers, A.3    Kluskens, L.D.4    Driessen, A.J.M.5    Kuipers, O.P.6
  • 38
    • 84873658266 scopus 로고    scopus 로고
    • A peptide derived from phage display library exhibits antibacterial activity against E. coli and Pseudomonas aeruginosa
    • Sainath Rao, S., Mohan, K. V. K., and Atreya, C. D. (2013). A peptide derived from phage display library exhibits antibacterial activity against E. coli and Pseudomonas aeruginosa. PLoS ONE 8:e56081. doi: 10.1371/journal.pone.0056081
    • (2013) PLoS ONE , vol.8
    • Sainath Rao, S.1    Mohan, K.V.K.2    Atreya, C.D.3
  • 40
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. (2006). Tricine-SDS-PAGE. Nat. Protoc. 1, 16-22. doi: 10.1038/nprot.2006.4
    • (2006) Nat. Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 41
    • 84871970730 scopus 로고    scopus 로고
    • Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
    • Torcato, I. M., Huang, Y.-H., Franquelim, H. G., Gaspar, D., Craik, D. J., Castanho, M. A., et al. (2013). Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria. Biochim. Biophys. Acta 1828, 944-955. doi: 10.1016/j.bbamem.2012.12.002
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 944-955
    • Torcato, I.M.1    Huang, Y.-H.2    Franquelim, H.G.3    Gaspar, D.4    Craik, D.J.5    Castanho, M.A.6
  • 42
    • 0027309021 scopus 로고
    • Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis
    • van der Meer, J. R., Polman, J., Beerthuyzen, M. M., Siezen, R. J., Kuipers, O. P., and de Vos, W. M. (1993). Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. J. Bacteriol. 175, 2578-2588
    • (1993) J. Bacteriol , vol.175 , pp. 2578-2588
    • van der Meer, J.R.1    Polman, J.2    Beerthuyzen, M.M.3    Siezen, R.J.4    Kuipers, O.P.5    de Vos, W.M.6
  • 44
    • 84879828226 scopus 로고    scopus 로고
    • Designing and producing modified, new-to-nature peptides with antimicrobial activity by use of a combination of various lantibiotic modification enzymes
    • van Heel, A. J., Mu, D., Montalbán-López, M., Hendriks, D., and Kuipers, O. P. (2013). Designing and producing modified, new-to-nature peptides with antimicrobial activity by use of a combination of various lantibiotic modification enzymes. ACS Synth. Biol. 2, 397-404. doi: 10.1021/sb3001084
    • (2013) ACS Synth. Biol , vol.2 , pp. 397-404
    • van Heel, A.J.1    Mu, D.2    Montalbán-López, M.3    Hendriks, D.4    Kuipers, O.P.5
  • 45
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000). The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008. doi: 10.1073/pnas.97.24.13003
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 46
    • 35848941716 scopus 로고    scopus 로고
    • Lantibiotics: peptides of diverse structure and function
    • Willey, J. M., and van der Donk, W. A. (2007). Lantibiotics: peptides of diverse structure and function. Annu. Rev. Microbiol. 61, 477-501. doi: 10.1146/annurev.micro.61.080706.093501
    • (2007) Annu. Rev. Microbiol , vol.61 , pp. 477-501
    • Willey, J.M.1    van der Donk, W.A.2
  • 47
    • 3142701459 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants
    • Yuan, J., Zhang, Z.-Z., Chen, X.-Z., Yang, W., and Huan, L.-D. (2004). Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants. Appl. Microbiol. Biotechnol. 64, 806-815. doi: 10.1007/s00253-004-1599-1
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , pp. 806-815
    • Yuan, J.1    Zhang, Z.-Z.2    Chen, X.-Z.3    Yang, W.4    Huan, L.-D.5
  • 48
    • 84927510430 scopus 로고    scopus 로고
    • The length of a lantibiotic hinge region has profound influence on antimicrobial activity and host specificity
    • Zhou, L., van Heel, A. J., and Kuipers, O. P. (2015). The length of a lantibiotic hinge region has profound influence on antimicrobial activity and host specificity. Front. Microbiol. 6:11. doi: 10.3389/fmicb.2015.00011
    • (2015) Front. Microbiol , vol.6 , pp. 11
    • Zhou, L.1    van Heel, A.J.2    Kuipers, O.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.