메뉴 건너뛰기




Volumn 27, Issue 6, 1996, Pages 467-479

Bacteriocins: Nature, function and structure

Author keywords

Bacteriocins; Bacterium typing; Bacterium like inhibitory substances; Bacterophage; Cloacins; Contracted forms; Pyocins; Relaxed forms

Indexed keywords

BACTERIOCIN;

EID: 0030390123     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-4328(96)00028-5     Document Type: Review
Times cited : (105)

References (110)
  • 1
    • 0028260623 scopus 로고
    • Analogies between superinfection exclusion and bacteriocin immunity
    • Alatossva, T., 1994. Analogies between superinfection exclusion and bacteriocin immunity. Trends Microbiol., 2, 215-216.
    • (1994) Trends Microbiol. , vol.2 , pp. 215-216
    • Alatossva, T.1
  • 2
    • 0027357192 scopus 로고
    • Evidence for association of bacteriocinogenic activity with membrane vesicles of Thermus rubens
    • Becker, R. J., Cooper, A. J. and Starzyka, M. J., 1993. Evidence for association of bacteriocinogenic activity with membrane vesicles of Thermus rubens. Microbios., 73, 123-133.
    • (1993) Microbios , vol.73 , pp. 123-133
    • Becker, R.J.1    Cooper, A.J.2    Starzyka, M.J.3
  • 4
    • 0000922085 scopus 로고
    • The structure of pyocin particles released from Pseudomonas aeruginosa by mitomycin C
    • Bradley, D. E., 1966. The structure of pyocin particles released from Pseudomonas aeruginosa by mitomycin C. Int. Congr. Elect. Microsc., 6, 115-116.
    • (1966) Int. Congr. Elect. Microsc. , vol.6 , pp. 115-116
    • Bradley, D.E.1
  • 5
    • 0014330312 scopus 로고
    • The structure and infective process of a contractile Pseudomonas aeruginosa bacteriophage
    • Bradley, D. E. and Robertson, D., 1968. The structure and infective process of a contractile Pseudomonas aeruginosa bacteriophage. J. Gen. Virol., 3, 247-254.
    • (1968) J. Gen. Virol. , vol.3 , pp. 247-254
    • Bradley, D.E.1    Robertson, D.2
  • 6
    • 0014180420 scopus 로고
    • Ultrastructure of bacteriophage and bacteriocins
    • Bradley, D., 1967. Ultrastructure of bacteriophage and bacteriocins. Bacteriol. Rev., 31, 230-314.
    • (1967) Bacteriol. Rev. , vol.31 , pp. 230-314
    • Bradley, D.1
  • 7
    • 0028325274 scopus 로고
    • Colicins, structure, mode of action, transfer through membranes and evolution
    • Braun, V., Pilsi, H. and Gross, P., 1994. Colicins, structure, mode of action, transfer through membranes and evolution. Arch. Microbiol., 161, 199-206.
    • (1994) Arch. Microbiol. , vol.161 , pp. 199-206
    • Braun, V.1    Pilsi, H.2    Gross, P.3
  • 8
    • 0000331264 scopus 로고
    • General introduction to the secretion of bacteriocins
    • James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series
    • Cavard, D. and Oudega, B., 1992. General introduction to the secretion of bacteriocins. In: Bacteriocins, Microcins and Lantíbiotics. James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series Vol 65. pp. 297-305.
    • (1992) Bacteriocins, Microcins and Lantíbiotics , vol.65 , pp. 297-305
    • Cavard, D.1    Oudega, B.2
  • 9
    • 0022653838 scopus 로고
    • Characterisation of the ColE9-J plasmid and analysis of its genetic organisation
    • Chak, K. F. and James, R., 1986. Characterisation of the ColE9-J plasmid and analysis of its genetic organisation. J. Gen. Microbiol., 132, 61-71.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 61-71
    • Chak, K.F.1    James, R.2
  • 10
    • 0001560786 scopus 로고
    • Efect of bactericidal substance from Staphylococcus aureus on group A streptococci II. Structural alterations
    • Clawson, C. C. and Dajani, A. S., 1970. Efect of bactericidal substance from Staphylococcus aureus on group A streptococci II. Structural alterations. Infect. Immun., 1, 491-498.
    • (1970) Infect. Immun. , vol.1 , pp. 491-498
    • Clawson, C.C.1    Dajani, A.S.2
  • 11
    • 0014236189 scopus 로고
    • Bacteriophage tail like particles associated with intra species killing of Proteus vulgaris
    • Coetzee, H. L., Coetzee, J. N. and Smit, J. A., 1968. Bacteriophage tail like particles associated with intra species killing of Proteus vulgaris. J. Gen. Virol., 2, 29-36.
    • (1968) J. Gen. Virol. , vol.2 , pp. 29-36
    • Coetzee, H.L.1    Coetzee, J.N.2    Smit, J.A.3
  • 12
    • 0016524407 scopus 로고
    • Genetic of resistance to colicins in Escherchia coli K-12: Cross-resistance among colicins of group B
    • Davies, J. K. and Reeves, P., 1975. Genetic of resistance to colicins in Escherchia coli K-12: cross-resistance among colicins of group B. J. Bacteriol., 123, 96-101.
    • (1975) J. Bacteriol. , vol.123 , pp. 96-101
    • Davies, J.K.1    Reeves, P.2
  • 13
    • 0016524407 scopus 로고
    • Genetic of resistance to colicins in Escherchia coli K-12: Cross-resistance among colicins of group B
    • Davies, J. K. and Reeves, P., 1975. Genetic of resistance to colicins in Escherchia coli K-12: cross-resistance among colicins of group B. J. Bacteriol., 123, 102-117.
    • (1975) J. Bacteriol. , vol.123 , pp. 102-117
    • Davies, J.K.1    Reeves, P.2
  • 14
    • 0000552682 scopus 로고
    • Plasmid-medicated prodction of staphylococcin in bacteriophage type 71 Staphylococcus aureus
    • Dajani, A. S., Taube, Z., 1974. Plasmid-medicated prodction of staphylococcin in bacteriophage type 71 Staphylococcus aureus. Antimicrob. Agents Chemother., 5, 594-598.
    • (1974) Antimicrob. Agents Chemother. , vol.5 , pp. 594-598
    • Dajani, A.S.1    Taube, Z.2
  • 15
    • 0011151742 scopus 로고
    • PhD thesis. Dublin University. Trinity College Dublin, Ireland
    • Daw, M. A., 1989. PhD thesis. Dublin University. Trinity College Dublin, Ireland.
    • (1989)
    • Daw, M.A.1
  • 16
  • 17
    • 0028302435 scopus 로고
    • Prevention of gram negative infections in neuropenic cancer patients
    • Daw, M. A. and Falkiner, F. R., 1994. Prevention of gram negative infections in neuropenic cancer patients. Saud. Med. J., 15, 196-203.
    • (1994) Saud. Med. J. , vol.15 , pp. 196-203
    • Daw, M.A.1    Falkiner, F.R.2
  • 18
    • 0026514902 scopus 로고
    • Application and assessment of cloacin typing of Enterobacter cloacae
    • Daw, M. A., Corcorn, G. D., Falkiner, F. R. and Keane, C. T., 1992. Application and assessment of cloacin typing of Enterobacter cloacae. J. Hosp. Infect., 20, 141-151.
    • (1992) J. Hosp. Infect. , vol.20 , pp. 141-151
    • Daw, M.A.1    Corcorn, G.D.2    Falkiner, F.R.3    Keane, C.T.4
  • 19
    • 0015694445 scopus 로고
    • Transport of vitamin B12 in Exherichia coli; common receptor sites for vitamin B12 and E colicins on the outer membrane of the cell envelop
    • Di Masi, R. D., White, J., Schaitman, C. A. and Bradbeer, C., 1973. Transport of vitamin B12 in Exherichia coli; common receptor sites for vitamin B12 and E colicins on the outer membrane of the cell envelop. J. Bacteriol., 115, 506-573.
    • (1973) J. Bacteriol. , vol.115 , pp. 506-573
    • Di Masi, R.D.1    White, J.2    Schaitman, C.A.3    Bradbeer, C.4
  • 20
    • 0014542423 scopus 로고
    • Infections due to Gram-negative organisms: An analysis of of 860 patients with bacteriamia at the university of Minnesota Medical Center, 1958-1966
    • Du Pont, H. L. and Spink, W. W., 1969. Infections due to Gram-negative organisms: an analysis of of 860 patients with bacteriamia at the university of Minnesota Medical Center, 1958-1966. Medicine, 48, 307-316.
    • (1969) Medicine , vol.48 , pp. 307-316
    • Du Pont, H.L.1    Spink, W.W.2
  • 21
    • 0015539879 scopus 로고
    • Segregation kinetics of colicinogenic factor Col E1 from a bacterial population temperature-sensitive for DNA polymerase 1
    • Durkacz, B. W. and Sherratt, D. J., 1973. Segregation Kinetics of colicinogenic factor Col E1 from a bacterial population temperature-sensitive for DNA polymerase 1. Mol. Gen. Genet., 121, 71-75.
    • (1973) Mol. Gen. Genet. , vol.121 , pp. 71-75
    • Durkacz, B.W.1    Sherratt, D.J.2
  • 22
    • 0015134932 scopus 로고
    • Structural changes in Colstridium botulinum type E after treatment with boticin S51
    • Ellison, J. S., Mattern, C. F. T. and Daniel, W. A., 1971. Structural changes in Colstridium botulinum type E after treatment with boticin S51. J. Bacteriol., 108, 526-534.
    • (1971) J. Bacteriol. , vol.108 , pp. 526-534
    • Ellison, J.S.1    Mattern, C.F.T.2    Daniel, W.A.3
  • 23
    • 0026906825 scopus 로고
    • Partially purified bacteriocin kills malignant cells by apoptosis: Programmed cell death
    • Farkas-Himsley, H., Zhang, Y. S., Yuan, M. and Musclow, C. E., 1992. Partially purified bacteriocin kills malignant cells by apoptosis: programmed cell death. Cell Mol. Biol. Noisy le grand. 38, 643-651.
    • (1992) Cell Mol. Biol. Noisy le Grand , vol.38 , pp. 643-651
    • Farkas-Himsley, H.1    Zhang, Y.S.2    Yuan, M.3    Musclow, C.E.4
  • 25
    • 0013768160 scopus 로고
    • On the nature of colicinogenic factors: A review
    • Fredericq, P., 1963. On the nature of colicinogenic factors: a review. J. Theor. Biol., 4, 159-161.
    • (1963) J. Theor. Biol. , vol.4 , pp. 159-161
    • Fredericq, P.1
  • 26
    • 0014865764 scopus 로고
    • Characterisation of Staphylococcus aureus bacteriocin
    • Gagliano, V. F. and Hindsill, R. D., 1970. Characterisation of Staphylococcus aureus bacteriocin. J. Bacteriol., 104, 117-125.
    • (1970) J. Bacteriol. , vol.104 , pp. 117-125
    • Gagliano, V.F.1    Hindsill, R.D.2
  • 27
    • 0344798303 scopus 로고
    • Immunity protein to pore forming colicins
    • James R. Lazdunski C and Pattus F. Springer-Verlag, Berlin. NATO ASI Series
    • Geli, V. and Lazdunski, C., 1992a. Immunity protein to pore forming colicins. In The Bacteriocin, Microcins and Lantibiotics by James R. Lazdunski C and Pattus F. pp 171-179. Springer-Verlag, Berlin. NATO ASI Series.
    • (1992) The Bacteriocin, Microcins and Lantibiotics , pp. 171-179
    • Geli, V.1    Lazdunski, C.2
  • 28
    • 0026688007 scopus 로고
    • An α-helical hydrophoic hairpin as a specific determinant in protein-protein interaction occuring in Escherichia coli colicin A and B immunity systems
    • Geli, V. and Lazdunski, C., 1992. An α-helical hydrophoic hairpin as a specific determinant in protein-protein interaction occuring in Escherichia coli colicin A and B immunity systems. J. Bacteriol., 147, 6432-6437.
    • (1992) J. Bacteriol. , vol.147 , pp. 6432-6437
    • Geli, V.1    Lazdunski, C.2
  • 29
    • 0000620353 scopus 로고
    • Sur un remarquable example d'antagonisme entre deux souches de colibacille
    • Gratia, A., 1925. sur un remarquable example d'antagonisme entre deux souches de colibacille. C. R. Soc. Biol., 93, 1040-1041.
    • (1925) C. R. Soc. Biol. , vol.93 , pp. 1040-1041
    • Gratia, A.1
  • 30
    • 0026813343 scopus 로고
    • Differential activity of bacteriocins and cefotaxime againist Serrutia marcescens clinical isolate SMG40 and its pigmented variant
    • Gratia, J. P. and Grenier, L., 1992. Differential activity of bacteriocins and cefotaxime againist Serrutia marcescens clinical isolate SMG40 and its pigmented variant. Int. J. Microbiol. Virol. Parasitol. Infect. Dis., 276, 340-346.
    • (1992) Int. J. Microbiol. Virol. Parasitol. Infect. Dis. , vol.276 , pp. 340-346
    • Gratia, J.P.1    Grenier, L.2
  • 31
    • 0026759604 scopus 로고
    • Brominated phosphplipids as for monitoring the memberane insertion of colicin A
    • Gonzalez-Manas, J. M., Lakey, J. H. and Pattus, F., 1992. Brominated phosphplipids as for monitoring the memberane insertion of colicin A. Biochemistry. 31, 7294-7300.
    • (1992) Biochemistry , vol.31 , pp. 7294-7300
    • Gonzalez-Manas, J.M.1    Lakey, J.H.2    Pattus, F.3
  • 32
  • 33
    • 0015983634 scopus 로고
    • Studies on the pyocins of Pseudomonas aeruginosa: Morphology and mode of action of contractile pyocins
    • Govan, J. R. W., 1974. Studies on the pyocins of Pseudomonas aeruginosa: morphology and mode of action of contractile pyocins. J. Gen. Micribiol. 80, 1-15.
    • (1974) J. Gen. Micribiol. , vol.80 , pp. 1-15
    • Govan, J.R.W.1
  • 34
    • 0015967448 scopus 로고
    • Studies on the pyocins of Pseudomonas aeruginosa: Production of contractiles and flexuous pyocins of Pseudomonas aeruginosa
    • Govan, J. R. W., 1974. Studies on the pyocins of Pseudomonas aeruginosa: production of contractiles and flexuous pyocins of Pseudomonas aeruginosa. J. Gen. Micribiol., 80, 15-30.
    • (1974) J. Gen. Micribiol. , vol.80 , pp. 15-30
    • Govan, J.R.W.1
  • 35
    • 0015873450 scopus 로고
    • Characterization of a bacteriocin from Staphylococcus aureus strain 462
    • Hale, E. M. and Hinsdill, R. D., 1973. Characterization of a bacteriocin from Staphylococcus aureus strain 462. Antimicrob. Agents Chemother., 4, 634-640.
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 634-640
    • Hale, E.M.1    Hinsdill, R.D.2
  • 36
    • 0016642533 scopus 로고
    • Colicinogeny and related phenomena
    • Hardy, K. G., 1975. Colicinogeny and related phenomena. Bacteriol. Rev., 39, 464-515.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 464-515
    • Hardy, K.G.1
  • 37
    • 0015458606 scopus 로고
    • Colicin factors and mitomycin-C
    • Hardy, K. G. and Meynell, G. G., 1972. Colicin factors and mitomycin-C. J. Gen. Microbiol., 73, 547-549.
    • (1972) J. Gen. Microbiol. , vol.73 , pp. 547-549
    • Hardy, K.G.1    Meynell, G.G.2
  • 38
    • 0015421039 scopus 로고
    • "Induction" of colicin factor E2-P9 by mitomycm C
    • Hardy, K. G. and Meynell, G. G., 1972. "Induction" of colicin factor E2-P9 by mitomycm C. J. Bacteriol., 112, 1007-1009.
    • (1972) J. Bacteriol. , vol.112 , pp. 1007-1009
    • Hardy, K.G.1    Meynell, G.G.2
  • 40
    • 0028017686 scopus 로고
    • The leader peptide of colicin V shares consenus sequence with leader peptides that are common among peptide bacteriocin produced by Gram positive bacteria
    • Havarstein, L. S., Holo, H. and Nes, I. F., 1994. The leader peptide of colicin V shares consenus sequence with leader peptides that are common among peptide bacteriocin produced by Gram positive bacteria. Microbiology. 140, 2383-2389.
    • (1994) Microbiology , vol.140 , pp. 2383-2389
    • Havarstein, L.S.1    Holo, H.2    Nes, I.F.3
  • 41
    • 0014531852 scopus 로고
    • Morphological studies on relaxed and contracted forms of purified pyocin particles
    • Higerd, T. B., Baechler, C. A. and Berk, R. S., 1969. Morphological studies on relaxed and contracted forms of purified pyocin particles. J. Bacteriol., 98, 1378-1389.
    • (1969) J. Bacteriol. , vol.98 , pp. 1378-1389
    • Higerd, T.B.1    Baechler, C.A.2    Berk, R.S.3
  • 42
    • 0024485644 scopus 로고
    • Aminoacid sequence and lenght requirements for assembly and function of the colicin A lysis protein
    • Howards, P., Cavard, D. and Lazdunski, C., 1989. Aminoacid sequence and lenght requirements for assembly and function of the colicin A lysis protein. J. Bacteriol., 171, 410-418.
    • (1989) J. Bacteriol. , vol.171 , pp. 410-418
    • Howards, P.1    Cavard, D.2    Lazdunski, C.3
  • 43
    • 85004435228 scopus 로고
    • Relationship between pyocins and a bacteriophage in pseudomonas aeruginosa
    • Ito, S. and Kageyama, M., 1970. Relationship between pyocins and a bacteriophage in pseudomonas aeruginosa. J. Gen. App. Microbiol., 16, 231-240.
    • (1970) J. Gen. App. Microbiol. , vol.16 , pp. 231-240
    • Ito, S.1    Kageyama, M.2
  • 44
    • 85004357627 scopus 로고
    • Isolation and characterisation of pyocins from several strains of Pseudomonas aeruginosa
    • Ito, K., Kageyama, M. and Egami, F., 1970. Isolation and characterisation of pyocins from several strains of Pseudomonas aeruginosa. J. Gen. Appl. Microbiol., 16, 205-214.
    • (1970) J. Gen. Appl. Microbiol. , vol.16 , pp. 205-214
    • Ito, K.1    Kageyama, M.2    Egami, F.3
  • 45
    • 0016181259 scopus 로고
    • Studies on the regulation of the colicin 1b synthsis: Replication of the Co1Ib-P9 plasmid during colicin induction
    • Issacson, R. E. and Konisky, J., 1974. studies on the regulation of the colicin 1b synthsis: replication of the Co1Ib-P9 plasmid during colicin induction. Antimicrob. Agents Chemother., 6, 848-852.
    • (1974) Antimicrob. Agents Chemother. , vol.6 , pp. 848-852
    • Issacson, R.E.1    Konisky, J.2
  • 46
    • 0015877358 scopus 로고
    • Production de bacteriocine liee a la presence d un plasmid chez Colistridium perferings type A
    • Ionesco, H. and Bouanchaud, D. H., 1973. Production de bacteriocine liee a la presence d un plasmid chez Colistridium perferings type A. C. R. Acad. Sci. (D) Paris, 276, 2855-2857.
    • (1973) C. R. Acad. Sci. (D) Paris , vol.276 , pp. 2855-2857
    • Ionesco, H.1    Bouanchaud, D.H.2
  • 47
    • 0003112428 scopus 로고
    • Bacteriocins and bacteriocin-like substances
    • Ivanovics, G., 1962. Bacteriocins and bacteriocin-like substances. Bacteriol. Rev., 26, 108-118.
    • (1962) Bacteriol. Rev. , vol.26 , pp. 108-118
    • Ivanovics, G.1
  • 48
    • 0026570237 scopus 로고
    • Factors affecting production of the group A streptococcus bacteriocin SA-FF22
    • Jack, R. W. and Tagg, J. R., 1992. Factors affecting production of the group A streptococcus bacteriocin SA-FF22. J. Med. Microbiol., 36, 132-138.
    • (1992) J. Med. Microbiol. , vol.36 , pp. 132-138
    • Jack, R.W.1    Tagg, J.R.2
  • 49
    • 77951352546 scopus 로고
    • Sur la biosynthese d'une colicine et sur son mode d'action
    • Jacob, F., Siminovitch, L. and Wollman, E., 1952. Sur la biosynthese d'une colicine et sur son mode d'action. Ann. Inst. Pasteur. 83, 295-315.
    • (1952) Ann. Inst. Pasteur. , vol.83 , pp. 295-315
    • Jacob, F.1    Siminovitch, L.2    Wollman, E.3
  • 50
    • 0011119619 scopus 로고
    • Specifity determination of the interaction between colicin E9 and its immunity protein
    • James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series, Springer-Verlag
    • James, R., Curtis, M. D., Wallis, R., Osborne, M., Kleanthous, C. and Moore, G. R., 1992. Specifity determination of the interaction between colicin E9 and its immunity protein. In: Bacteriocins, Microcins and lantibiotics James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series Vol 65, Springer-Verlag, pp. 181-201.
    • (1992) Bacteriocins, Microcins and Lantibiotics , vol.65 , pp. 181-201
    • James, R.1    Curtis, M.D.2    Wallis, R.3    Osborne, M.4    Kleanthous, C.5    Moore, G.R.6
  • 51
    • 0002439915 scopus 로고
    • Bacteriocins and bacteriophages of Pseudomonas aeruginosa
    • Mitsubashi, S. and Hashimoto, H. (eds). University of Tokyo Press, Tokyo
    • Kageyama, M., 1975. Bacteriocins and bacteriophages of Pseudomonas aeruginosa. In: Microbial Drug Resistance, Mitsubashi, S. and Hashimoto, H. (eds). University of Tokyo Press, Tokyo. pp. 291-305.
    • (1975) Microbial Drug Resistance , pp. 291-305
    • Kageyama, M.1
  • 52
    • 0001052911 scopus 로고
    • On the purification and some properties of a pyocin-bacteriocin produced by Pseudomonas aeruginosa
    • Kageyama, M. and Egami, F., 1962. On the purification and some properties of a pyocin-bacteriocin produced by Pseudomonas aeruginosa. Life Sci., 9, 471-476.
    • (1962) Life Sci. , vol.9 , pp. 471-476
    • Kageyama, M.1    Egami, F.2
  • 53
    • 0013780674 scopus 로고
    • Studies on the mode of action of pyocin. I. Inhibition of macromloecular synthesis in sensitive cells
    • Kaziro, Y. and Tanaka, M., 1965. Studies on the mode of action of pyocin. I. Inhibition of macromloecular synthesis in sensitive cells. J. Biochem., 57, 689-695.
    • (1965) J. Biochem. , vol.57 , pp. 689-695
    • Kaziro, Y.1    Tanaka, M.2
  • 54
    • 0013806358 scopus 로고
    • Studies on the mode of action of pyocin II inactivation of ribosomes
    • Kaziro, Y. and Tanaka, M., 1965. Studies on the mode of action of pyocin II Inactivation of ribosomes. J. Biochem., 58, 357-363.
    • (1965) J. Biochem. , vol.58 , pp. 357-363
    • Kaziro, Y.1    Tanaka, M.2
  • 55
    • 0014219704 scopus 로고
    • Structure of the normal and contracted tail sheaths of T4 bacteiophage
    • Krimm, S. and Anderson, A. F., 1967. Structure of the normal and contracted tail sheaths of T4 bacteiophage. J. Mol. Biol., 27, 197-202.
    • (1967) J. Mol. Biol. , vol.27 , pp. 197-202
    • Krimm, S.1    Anderson, A.F.2
  • 56
    • 0013911949 scopus 로고
    • Bacteriocin production by strains of Neisseria meningitidis
    • Kingsbury, D., 1966. Bacteriocin production by strains of Neisseria meningitidis. J. Bacteriol., 91, 1696-1699.
    • (1966) J. Bacteriol. , vol.91 , pp. 1696-1699
    • Kingsbury, D.1
  • 57
    • 0027450611 scopus 로고
    • Insertion derivatives containing segments of up to 16 amino acids identify surface and periplasm-exposed regions of the outer memberane receptor of Escherichia coli K-12
    • Koebink, R. and Braun, V., 1993. Insertion derivatives containing segments of up to 16 amino acids identify surface and periplasm-exposed regions of the outer memberane receptor of Escherichia coli K-12. J. Bacteriol., 3, 826-839.
    • (1993) J. Bacteriol. , vol.3 , pp. 826-839
    • Koebink, R.1    Braun, V.2
  • 59
    • 0020350235 scopus 로고
    • Colicins and other bacteriocins with established modes of action
    • Konisky, J., 1982. Colicins and other bacteriocins with established modes of action. Ann. Rev. Microbiol., 36, 125-145.
    • (1982) Ann. Rev. Microbiol. , vol.36 , pp. 125-145
    • Konisky, J.1
  • 60
    • 0014939624 scopus 로고
    • Characterisation of colicin Ia and colicin Ib
    • Konisky, R. and Richard, S. F., 1970. Characterisation of colicin Ia and colicin Ib. J. Biol. Chem., 245, 2972-2978.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2972-2978
    • Konisky, R.1    Richard, S.F.2
  • 61
    • 0027157448 scopus 로고
    • Flouresence energy transfer distance measurements the hydrophopic helical hairpin of colicin A in the membrane bound state
    • Lakey, J. H., Duche, D., Gonzalez-Manas, J. M., Baty, D. and Pattus, F., 1993. Flouresence energy transfer distance measurements the hydrophopic helical hairpin of colicin A in the membrane bound state. J. Mol. Biol., 230, 1055-1067.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1055-1067
    • Lakey, J.H.1    Duche, D.2    Gonzalez-Manas, J.M.3    Baty, D.4    Pattus, F.5
  • 63
    • 0027351878 scopus 로고
    • Antibacterial spectrum of bacteriocin-like substances produced by rumen staphylococci
    • Laukova, A. and Marekova, M., 1993. Antibacterial spectrum of bacteriocin-like substances produced by rumen staphylococci. Folia Microbiol. Praha., 38, 74-76.
    • (1993) Folia Microbiol. Praha. , vol.38 , pp. 74-76
    • Laukova, A.1    Marekova, M.2
  • 64
    • 0027550912 scopus 로고
    • A method of typing Listeria monocytogenes strains by classification of listeriocin and phage receptors
    • Lebek, G., Teysseire, P. and Baugartner, A., 1993. A method of typing Listeria monocytogenes strains by classification of listeriocin and phage receptors. Int. J. Microbiol. Virol. Parasitol. Infect. Dis., 278, 58-65.
    • (1993) Int. J. Microbiol. Virol. Parasitol. Infect. Dis. , vol.278 , pp. 58-65
    • Lebek, G.1    Teysseire, P.2    Baugartner, A.3
  • 65
    • 0026569555 scopus 로고
    • The hemolysin/bacteriocin produced by enterococci is a marker of pathogenicity
    • Libertin, C. R., Dumitru, R. and Stein, D. S., 1992. The hemolysin/bacteriocin produced by enterococci is a marker of pathogenicity. Diagn. Microbiol. Infect. Dis., 15, 115-120.
    • (1992) Diagn. Microbiol. Infect. Dis. , vol.15 , pp. 115-120
    • Libertin, C.R.1    Dumitru, R.2    Stein, D.S.3
  • 66
    • 0026580005 scopus 로고
    • Purification and characterisation of extracellular mutacin, abacteriocin Streptococcus sorbinus
    • Loyola-Rodriguez, J. P., Morisaki, I., Kitamura, K. and Hamada, S., 1992. Purification and characterisation of extracellular mutacin, abacteriocin Streptococcus sorbinus. J. Gen. Microbiol., 138, 269-274.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 269-274
    • Loyola-Rodriguez, J.P.1    Morisaki, I.2    Kitamura, K.3    Hamada, S.4
  • 67
    • 0015416460 scopus 로고
    • Effects of colicins E1 and K on permeability to magnesium and cobaltous ions
    • Lusk, J. E. and Nelson, D. L., 1972. Effects of colicins E1 and K on permeability to magnesium and cobaltous ions. J. Bacteriol., 112, 148-160.
    • (1972) J. Bacteriol. , vol.112 , pp. 148-160
    • Lusk, J.E.1    Nelson, D.L.2
  • 69
    • 77956856274 scopus 로고
    • Methods for studying bacteriocins
    • Norris, J. R. and Ribbons, D. W. (eds). Academic Press
    • Mayr-Harting, A., Hedges, A. J., and Berkeley, R. C. W., 1972. Methods for studying bacteriocins. In: Methods in Microbiology, Norris, J. R. and Ribbons, D. W. (eds). Academic Press, pp. 315-422.
    • (1972) Methods in Microbiology , pp. 315-422
    • Mayr-Harting, A.1    Hedges, A.J.2    Berkeley, R.C.W.3
  • 70
    • 0027481708 scopus 로고
    • Purification and partial characterisation of a bacteriocin isolated from Bacteroides ovatus H 47
    • Miranda, C. M., 1993. Purification and partial characterisation of a bacteriocin isolated from Bacteroides ovatus H 47. Can. J. Microbiol., 39, 169-174.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 169-174
    • Miranda, C.M.1
  • 71
    • 0028605699 scopus 로고
    • Evidence that dissipation of proton motive force is a common mechanism of action for bacteriocins and other antimicrobial proteins
    • Montville, T. J. and Bruno, M. E. C., 1995. Evidence that dissipation of proton motive force is a common mechanism of action for bacteriocins and other antimicrobial proteins. Int. J. Food Microbiol. 24, 53-59.
    • (1995) Int. J. Food Microbiol. , vol.24 , pp. 53-59
    • Montville, T.J.1    Bruno, M.E.C.2
  • 72
    • 0014219440 scopus 로고
    • Structure of the sheath of bacteriophage T4, I. Structure of the contracted sheath and polysheath
    • Moody, M. F., 1967. Structure of the sheath of bacteriophage T4, I. Structure of the contracted sheath and polysheath. J. Mol. Biol., 25, 167-200.
    • (1967) J. Mol. Biol. , vol.25 , pp. 167-200
    • Moody, M.F.1
  • 73
    • 0014219345 scopus 로고
    • Structure of the sheath of bacteriophage T4, II. Rearrangement of the sheath subunits during contraction
    • Moody, M. F., 1967. Structure of the sheath of bacteriophage T4, II. Rearrangement of the sheath subunits during contraction. J. Mol. Biol., 25, 201-208.
    • (1967) J. Mol. Biol. , vol.25 , pp. 201-208
    • Moody, M.F.1
  • 74
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto-Lozano, J. C., Meyer, J. N., Sletten, K., Pleaz, C. and Nes, I. F., 1992. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol., 138, 1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto-Lozano, J.C.1    Meyer, J.N.2    Sletten, K.3    Pleaz, C.4    Nes, I.F.5
  • 75
    • 0014047739 scopus 로고
    • Colicins and related bacteriocins
    • Nomura, M., 1967. Colicins and related bacteriocins. Ann. Rev. Microbiol., 12, 257-284.
    • (1967) Ann. Rev. Microbiol. , vol.12 , pp. 257-284
    • Nomura, M.1
  • 76
    • 0015581703 scopus 로고
    • Purification and properties of pyocin S2
    • Ohkawa, I., Kageyama, M. and Egami, F., 1973. Purification and properties of pyocin S2. J. Biochem., 73, 281-289.
    • (1973) J. Biochem. , vol.73 , pp. 281-289
    • Ohkawa, I.1    Kageyama, M.2    Egami, F.3
  • 77
    • 0017712149 scopus 로고
    • Purifecation and characterisation of active component and active fragment of Colicin E3
    • Ohno, S., Ohno-Iwashita, Y., Suzuki, K. and Imahori, K., 1977. Purifecation and characterisation of active component and active fragment of Colicin E3. J. Biochem. (Tokyo), 82, 1045-1053.
    • (1977) J. Biochem. (Tokyo) , vol.82 , pp. 1045-1053
    • Ohno, S.1    Ohno-Iwashita, Y.2    Suzuki, K.3    Imahori, K.4
  • 78
    • 0026709119 scopus 로고
    • Identification and characterisation of two bacteriocin-producing strains of Lactococcus lactis isolated from vegetables
    • Unlman, L., Schillinger, U., Rupnow, J. R. and Holzapfel, W. H., 1992. Identification and characterisation of two bacteriocin-producing strains of Lactococcus lactis isolated from vegetables. Int. J. Food Microbiol., 16, 141-151.
    • (1992) Int. J. Food Microbiol. , vol.16 , pp. 141-151
    • Unlman, L.1    Schillinger, U.2    Rupnow, J.R.3    Holzapfel, W.H.4
  • 79
    • 0024961641 scopus 로고
    • Structure of the membrane forming fragment of the colicin A
    • Parker, M. W., Pattus, F., Tucker, A. D. and Tsernoglou, D., 1989. Structure of the membrane forming fragment of the colicin A. Nature, 337, 93-96.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsernoglou, D.4
  • 80
    • 0019119131 scopus 로고
    • State of the art: Typing Pseudomonas aeruginosa
    • Pitt, T. L., 1980. State of the art: typing Pseudomonas aeruginosa. J. Hosp. Infect., 1, 195-1101.
    • (1980) J. Hosp. Infect. , vol.1 , pp. 195-1101
    • Pitt, T.L.1
  • 81
    • 0028174190 scopus 로고
    • Bacteriocin plasmid pMB1 of Enterococcus faecalis, identification of the cell aggregation substances after induction by sex pheromone
    • Quirantes, R., Martin, I., Valdiva, E., Galvez, A., Martinez-Bueno, M. and Moqueda, M., 1994. Bacteriocin plasmid pMB1 of Enterococcus faecalis, identification of the cell aggregation substances after induction by sex pheromone. Can. J. Microbiol., 40, 500-503.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 500-503
    • Quirantes, R.1    Martin, I.2    Valdiva, E.3    Galvez, A.4    Martinez-Bueno, M.5    Moqueda, M.6
  • 82
    • 0002665597 scopus 로고
    • The bacteriocins
    • Reeves, P., 1965. The bacteriocins. Bacteriol. Rev., 29, 24-45.
    • (1965) Bacteriol. Rev. , vol.29 , pp. 24-45
    • Reeves, P.1
  • 84
    • 0002393567 scopus 로고
    • Pyocins S1 and S2, bacteriocins of Pseudomonas aeruginosa
    • Silver, S., Chakrabarty, A. M., Iglewski, B. and Kalpans, E. (eds). American Society of Microbiology. Washington, DC
    • Sano, Y., Matsui, H., Kobayashi, M. and Kageyama, M., 1990. Pyocins S1 and S2, bacteriocins of Pseudomonas aeruginosa. In: Pseudomonas, biotransformation, pathogensis, Silver, S., Chakrabarty, A. M., Iglewski, B. and Kalpans, E. (eds). American Society of Microbiology. Washington, DC, pp. 352-358.
    • (1990) Pseudomonas, Biotransformation, Pathogensis , pp. 352-358
    • Sano, Y.1    Matsui, H.2    Kobayashi, M.3    Kageyama, M.4
  • 85
    • 0027155821 scopus 로고
    • Molecular structure and functions of pyocins S1 and S2 in Pseudomonas aeruginosa
    • Sano, Y., Matsui, H., Kobayashi, M. and Kageyama, M., 1993. Molecular structure and functions of pyocins S1 and S2 in Pseudomonas aeruginosa. J. Bacteriol., 175, 2907-2916.
    • (1993) J. Bacteriol. , vol.175 , pp. 2907-2916
    • Sano, Y.1    Matsui, H.2    Kobayashi, M.3    Kageyama, M.4
  • 86
    • 0019826294 scopus 로고
    • Purification and properties of an S-type pyocin, pyocin AP41
    • Sano, Y. and Kageyama, M., 1981. Purification and properties of an S-type pyocin, pyocin AP41. J. Bacteriol., 146, 733-739.
    • (1981) J. Bacteriol. , vol.146 , pp. 733-739
    • Sano, Y.1    Kageyama, M.2
  • 87
    • 0021326862 scopus 로고
    • Genetic determinant of pyocin AP41 and an insert in the Pseudomonas aeruginosa chromosome
    • Sano, Y. and Kageyama, M., 1984. Genetic determinant of pyocin AP41 and an insert in the Pseudomonas aeruginosa chromosome. J. Bacteriol., 158, 562-570.
    • (1984) J. Bacteriol. , vol.158 , pp. 562-570
    • Sano, Y.1    Kageyama, M.2
  • 88
    • 0018236743 scopus 로고
    • Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes
    • Schein, S. J., Kagan, B. B. and Finkelstein, A., 1978. Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature, 276, 159-163.
    • (1978) Nature , vol.276 , pp. 159-163
    • Schein, S.J.1    Kagan, B.B.2    Finkelstein, A.3
  • 89
    • 0016223157 scopus 로고
    • Transcription of the Co1E1 genome in colicinogenic Esherichia coli strains during induction with mitomycin C
    • Schiess, W. and Goebel, W., 1974. Transcription of the Co1E1 genome in colicinogenic Esherichia coli strains during induction with mitomycin C. FEBS Lett., 47, 356-359.
    • (1974) FEBS Lett. , vol.47 , pp. 356-359
    • Schiess, W.1    Goebel, W.2
  • 90
    • 0027398487 scopus 로고
    • Purification, partial characterisation and plasmid-linkage of pediocin SJ-1, a bacteriocin produced by Pepdiococcous acidilactici
    • Schved, F., Lalazar, A., Henis, Y. and Juven, B. V., 1993. Purification, partial characterisation and plasmid-linkage of pediocin SJ-1, a bacteriocin produced by Pepdiococcous acidilactici. J. Appl. Bacteriol., 74, 67-77.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 67-77
    • Schved, F.1    Lalazar, A.2    Henis, Y.3    Juven, B.V.4
  • 91
    • 0015240291 scopus 로고
    • Purification and characterisation of colicin E1
    • Schwartz, S. A. and Helinski, D. R., 1971. Purification and characterisation of colicin E1. J. Biol. Chem., 246, 6318-6327.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6318-6327
    • Schwartz, S.A.1    Helinski, D.R.2
  • 92
    • 0020527441 scopus 로고
    • Genetic determinant of pyocin R2 in Pseudomonas aeruginosa PAO, I. Localisation of the pyocin R2 gene cluster between the trp CD and trp E genes
    • Shinomiya, T., Shiga, S. and Kageyama, M., 1983. Genetic determinant of pyocin R2 in Pseudomonas aeruginosa PAO, I. Localisation of the pyocin R2 gene cluster between the trp CD and trp E genes. Mol. Gen. Genet., 189, 375-381.
    • (1983) Mol. Gen. Genet. , vol.189 , pp. 375-381
    • Shinomiya, T.1    Shiga, S.2    Kageyama, M.3
  • 93
    • 0026439333 scopus 로고
    • Production of bactenocin inhibitory to Listeria species by Enterococcous hirae
    • Siragusa, G. R., 1992. Production of bactenocin inhibitory to Listeria species by Enterococcous hirae. Appl. Environ. Microbiol., 58, 3508-3513.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3508-3513
    • Siragusa, G.R.1
  • 94
    • 0001311435 scopus 로고
    • Structural studies on colicins E3 and its immunity protein
    • James R., Lazdunski, C. and Pattus, F. (eds). NATO ASI Series
    • Soham, M. and Djebli, A., 1992. Structural studies on colicins E3 and its immunity protein. In: Bacteriocins, microcins and lantibiotics James R., Lazdunski, C. and Pattus, F. (eds). NATO ASI Series, pp. 203-214.
    • (1992) Bacteriocins, Microcins and Lantibiotics , pp. 203-214
    • Soham, M.1    Djebli, A.2
  • 95
    • 0028508049 scopus 로고
    • Bacteriocins produced by Leuconostocs species
    • Stiles, M. E., 1994. Bacteriocins produced by Leuconostocs species. J. Dairy Sci., 77, 2718-2722.
    • (1994) J. Dairy Sci. , vol.77 , pp. 2718-2722
    • Stiles, M.E.1
  • 96
    • 0027474607 scopus 로고
    • Characterisation of bacteriocin produced by Pediococcus pentosacceus from wine
    • Strasser de-Saad, M. A. and Hanea de-Nadra, M. C., 1993. Characterisation of bacteriocin produced by Pediococcus pentosacceus from wine. J. Appl. Bacteriol., 74, 406-410.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 406-410
    • Strasser De-Saad, M.A.1    Hanea De-Nadra, M.C.2
  • 98
    • 0003152675 scopus 로고
    • Bacteriocins of Gram-positive bacteria; an opinion regarding their nature, nomenclature, and numbers
    • James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series
    • Tagg, J. R., 1992. Bacteriocins of Gram-positive bacteria; an opinion regarding their nature, nomenclature, and numbers. In: Bacteriocins, microcins and lantibiotics. James, R., Lazdunski, C. and Pattus, F. (eds). NATO ASI series, pp. 33-36.
    • (1992) Bacteriocins, Microcins and Lantibiotics , pp. 33-36
    • Tagg, J.R.1
  • 99
    • 0015856163 scopus 로고
    • Morphological changes in a susceptible strain of Streptococcus pyogenes treated with streptocin A
    • Tagg, J. R., Pihl, E. A. and McGiven, A. R., 1973. Morphological changes in a susceptible strain of Streptococcus pyogenes treated with streptocin A. J. Gen. Microbiol., 79, 167-169.
    • (1973) J. Gen. Microbiol. , vol.79 , pp. 167-169
    • Tagg, J.R.1    Pihl, E.A.2    McGiven, A.R.3
  • 100
    • 0011142467 scopus 로고
    • Mycobacteriocin classification of rapidly growing mycobacteria
    • Takeya, K. and Tokiwa, H., 1972. Mycobacteriocin classification of rapidly growing mycobacteria. Int. J. Syst. Bacteriol., 22, 178-180.
    • (1972) Int. J. Syst. Bacteriol. , vol.22 , pp. 178-180
    • Takeya, K.1    Tokiwa, H.2
  • 101
    • 0016199883 scopus 로고
    • Bacteriocin typing of Mycobacterium tuberculosis
    • Takeya, K. and Tokiwa, H., 1974. Bacteriocin typing of Mycobacterium tuberculosis. Am. Rev. Respir. Dis., 109, 304-305.
    • (1974) Am. Rev. Respir. Dis. , vol.109 , pp. 304-305
    • Takeya, K.1    Tokiwa, H.2
  • 102
    • 0018265545 scopus 로고
    • In-vitro deploarization of Escherichia coli membrane vesicles by colicin Ia
    • Tokuda, H. and Konisky, J., 1978. In-vitro deploarization of Escherichia coli membrane vesicles by colicin Ia. J. Biol. Chem., 253, 7731-7737.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7731-7737
    • Tokuda, H.1    Konisky, J.2
  • 103
    • 0345061582 scopus 로고
    • Virulence plasmids
    • Hardy, K. G. (ed.). The practical approach series, IRL press. Oxford University Press
    • Tolmasky, M. E., Actis, L. A. and Crosa, J. H., 1993. Virulence plasmids. In: Plasmids. Hardy, K. G. (ed.). The practical approach series, IRL press. Oxford University Press, pp. 95-118.
    • (1993) Plasmids , pp. 95-118
    • Tolmasky, M.E.1    Actis, L.A.2    Crosa, J.H.3
  • 104
    • 0025932041 scopus 로고
    • A 'molten-globule' membrene insertion intermediate of the pore-forming domain of colicin A
    • van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H. and Pattus, F., 1991. A 'molten-globule' membrene insertion intermediate of the pore-forming domain of colicin A. Nature. 354, 408-410.
    • (1991) Nature , vol.354 , pp. 408-410
    • Van Der Goot, F.G.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 105
    • 0026313017 scopus 로고
    • Colicin E1 export in Salmonella typhimurium wild-type and lipopolysaccharide mutants
    • Viejo, B. M., Regue, M., Camprubi, S. and Tomas, J. M., 1991. Colicin E1 export in Salmonella typhimurium wild-type and lipopolysaccharide mutants. Folia. Microbiol. Praha., 36, 317-318.
    • (1991) Folia. Microbiol. Praha. , vol.36 , pp. 317-318
    • Viejo, B.M.1    Regue, M.2    Camprubi, S.3    Tomas, J.M.4
  • 106
    • 0028558959 scopus 로고
    • Isolation and characterisation of two bacteriocins produced by Enterococcus faecium strains inhibitory to Listeria monocytogenes
    • Vlaemynck, G., Herman, L. and Coudijzer, K., 1995. Isolation and characterisation of two bacteriocins produced by Enterococcus faecium strains inhibitory to Listeria monocytogenes. Int. J. Food Microbiol. 24, 211-217.
    • (1995) Int. J. Food Microbiol. , vol.24 , pp. 211-217
    • Vlaemynck, G.1    Herman, L.2    Coudijzer, K.3
  • 107
    • 0025372570 scopus 로고
    • Tol C, an Escherichia coli outer memberane protein required for haemolysin secretion
    • Wandersman, C. and Delepelaire, P., 1990. Tol C, an Escherichia coli outer memberane protein required for haemolysin secretion. Proc. Natn Acad. Sci. USA, 87, 4776-4780.
    • (1990) Proc. Natn Acad. Sci. USA , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 108
    • 0019464086 scopus 로고
    • Mode of action of colicin 1b. Formation of ion-permeable memberane channels
    • Weaver, C. A., Kagan, B. L., Finkelstein, A. and Konisky, J., 1981. Mode of action of colicin 1b. formation of ion-permeable memberane channels. Biochem. Biophys. Acta. 645, 137-142.
    • (1981) Biochem. Biophys. Acta , vol.645 , pp. 137-142
    • Weaver, C.A.1    Kagan, B.L.2    Finkelstein, A.3    Konisky, J.4
  • 109
    • 0019867469 scopus 로고
    • Plasmid detremined immunity of Escherichia coli K-12 to colicin Ia is mediated by plasmid encoded membrane protein
    • Weaver, C. A., Redborg, A. H. and Konisky, J., 1981. Plasmid detremined immunity of Escherichia coli K-12 to colicin Ia is mediated by plasmid encoded membrane protein. J. Bacteriol., 148, 817-828.
    • (1981) J. Bacteriol. , vol.148 , pp. 817-828
    • Weaver, C.A.1    Redborg, A.H.2    Konisky, J.3
  • 110
    • 0026628171 scopus 로고
    • The secondary structure of the colicin E3 immunity protein as studied by 1H-1H and 1H and 15 N two dimensional NMR spectroscopy
    • Yajima, S., Muto, Y., Yokoyama Masaki, H. and Uozumi, T., 1992. The secondary structure of the colicin E3 immunity protein as studied by 1H-1H and 1H and 15 N two dimensional NMR spectroscopy. Biochemistry. 31, 5578-5586
    • (1992) Biochemistry , vol.31 , pp. 5578-5586
    • Yajima, S.1    Muto, Y.2    Yokoyama Masaki, H.3    Uozumi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.