메뉴 건너뛰기




Volumn 280, Issue 4, 1998, Pages 583-596

The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death

Author keywords

Antibiotics; Lipoproteins; Osmoregulation; Programmed cell death; Stationary phase

Indexed keywords

LIPOPROTEIN; SIGMA FACTOR;

EID: 0032563108     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1894     Document Type: Article
Times cited : (83)

References (69)
  • 1
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal "addiction moduleregulated by guanosine-3′,5′-bispyrophosphate: A model for programmed bacterial cell death
    • Aizenman, E., Engelberg-Kulka, H. & Glaser, G. (1996). An Escherichia coli chromosomal "addiction moduleregulated by guanosine-3′,5′-bispyrophosphate: a model for programmed bacterial cell death. Proc. Natl Acad. Sci. USA, 93, 6059-6063.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-Kulka, H.2    Glaser, G.3
  • 3
    • 0029893702 scopus 로고    scopus 로고
    • The origin of programmed cell death
    • Ameisen, J. C. (1996). The origin of programmed cell death. Science, 272, 1278-1279.
    • (1996) Science , vol.272 , pp. 1278-1279
    • Ameisen, J.C.1
  • 4
    • 0026048799 scopus 로고
    • Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis
    • Aoki, H., Adams, S. L., Chung, D. G., Yaguchi, M., Chuang, S. E. & Ganoza, M. C. (1991). Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis. Nucl. Acids Res. 19, 6215-6220.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 6215-6220
    • Aoki, H.1    Adams, S.L.2    Chung, D.G.3    Yaguchi, M.4    Chuang, S.E.5    Ganoza, M.C.6
  • 6
    • 0027447435 scopus 로고
    • Overproduction, solubilization, purification and DNA-binding properties of AmpR from Citrobacter freundii
    • Bishop, R. E. & Weiner, J. H. (1993a). Overproduction, solubilization, purification and DNA-binding properties of AmpR from Citrobacter freundii. Eur. J. Biochem. 213, 405-412.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 405-412
    • Bishop, R.E.1    Weiner, J.H.2
  • 7
    • 0027495480 scopus 로고
    • Complementation of growth defect in an ampC deletion mutant of Escherichia coli
    • Bishop, R. E. & Weiner, J. H. (1993b). Complementation of growth defect in an ampC deletion mutant of Escherichia coli. FEMS Microbiol. Letters, 114, 349-354.
    • (1993) FEMS Microbiol. Letters , vol.114 , pp. 349-354
    • Bishop, R.E.1    Weiner, J.H.2
  • 8
    • 0029112604 scopus 로고
    • Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D: Implications for the origin of lipocalins
    • Bishop, R. E., Penfold, S. S., Frost, L. S., Höltje, J-.V. & Weiner, J. H. (1995). Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D: implications for the origin of lipocalins. J. Biol. Chem. 270, 23097-23103.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23097-23103
    • Bishop, R.E.1    Penfold, S.S.2    Frost, L.S.3    Höltje, J.-V.4    Weiner, J.H.5
  • 10
    • 0022970773 scopus 로고
    • Evolution of the apolipoproteins: Structure of the rat apo-A-IV gene and its relationship to the human genes for apo-A-I, C-III, and E
    • Boguski, M. S., Birkenmeier, E. H., Elshourbagy, N. A., Taylor, J. M. & Gordon, J. I. (1986). Evolution of the apolipoproteins: structure of the rat apo-A-IV gene and its relationship to the human genes for apo-A-I, C-III, and E. J. Biol. Chem. 261, 6398-6407.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6398-6407
    • Boguski, M.S.1    Birkenmeier, E.H.2    Elshourbagy, N.A.3    Taylor, J.M.4    Gordon, J.I.5
  • 11
    • 0027940025 scopus 로고
    • New genes in old sequences: A strategy for finding genes in the bacterial genome
    • Borodovsky, M., Koonin, E. V. & Rudd, K. E. (1994). New genes in old sequences: a strategy for finding genes in the bacterial genome. Trends Biochem. Sci. 19, 309-313.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 309-313
    • Borodovsky, M.1    Koonin, E.V.2    Rudd, K.E.3
  • 12
    • 0029073731 scopus 로고
    • Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92. 8 through 100 minutes
    • Burland, V., Plunkett, G., Sofia, H. J., Daniels, D. L. & Blattner, F. R. (1995). Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92. 8 through 100 minutes. Nucl. Acids Res. 23, 2105-2119.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2105-2119
    • Burland, V.1    Plunkett, G.2    Sofia, H.J.3    Daniels, D.L.4    Blattner, F.R.5
  • 13
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage, lambda and Mu
    • Casadaban, M. (1976). Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage, lambda and Mu. J. Mol. Biol. 104, 541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.1
  • 14
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J. & Cohen, S. N. (1980). Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 16
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand, R. M., Shai, Y., Segrest, J. P. & Anantharamaiah, G. M. (1995). Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers, 37, 319-338.
    • (1995) Biopolymers , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 18
    • 0031576356 scopus 로고    scopus 로고
    • Programmed cell death by hok/sok of plasmid R1: Processing of the hok mRNA 3′-end triggers structural rearrangements that allow translation and antisense RNA binding
    • Franch, T., Gultyaev, A. P. & Gerdes, K. (1997). Programmed cell death by hok/sok of plasmid R1: processing of the hok mRNA 3′-end triggers structural rearrangements that allow translation and antisense RNA binding. J. Mol. Biol. 273, 38-51.
    • (1997) J. Mol. Biol. , vol.273 , pp. 38-51
    • Franch, T.1    Gultyaev, A.P.2    Gerdes, K.3
  • 19
    • 0026010463 scopus 로고
    • The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity
    • Gennity, J. M. & Inouye, M. (1991). The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity. J. Biol. Chem. 266, 16458-16464.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16458-16464
    • Gennity, J.M.1    Inouye, M.2
  • 20
    • 0027410577 scopus 로고
    • A novel multicopy suppressor of a groEL mutation includes two nested open reading frames transcribed from different promoters
    • Greener, T., Govezensky, D. & Zamir, A. (1993). A novel multicopy suppressor of a groEL mutation includes two nested open reading frames transcribed from different promoters. EMBO J. 12, 889-896.
    • (1993) EMBO J. , vol.12 , pp. 889-896
    • Greener, T.1    Govezensky, D.2    Zamir, A.3
  • 21
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G. D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 22
    • 0031576339 scopus 로고    scopus 로고
    • Programmed cell death by hok/sok of plasmid R1: Coupled nucleotide covariations reveal a phylogenetically conserved folding pathway in the hok family of mRNAs
    • Gultyaev, A. P., Franch, T. & Gerdes, K. (1997). Programmed cell death by hok/sok of plasmid R1: coupled nucleotide covariations reveal a phylogenetically conserved folding pathway in the hok family of mRNAs. J. Mol. Biol. 273, 26-37.
    • (1997) J. Mol. Biol. , vol.273 , pp. 26-37
    • Gultyaev, A.P.1    Franch, T.2    Gerdes, K.3
  • 23
    • 0029807112 scopus 로고    scopus 로고
    • Cloning and expression of the gene for serine-glyoxalate aminotransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2
    • Hagishita, T., Yoshida, T., Izumi, Y. & Mitsunaga, T. (1996). Cloning and expression of the gene for serine-glyoxalate aminotransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2. Eur. J. Biochem. 241, 1-5.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 1-5
    • Hagishita, T.1    Yoshida, T.2    Izumi, Y.3    Mitsunaga, T.4
  • 24
    • 0028875660 scopus 로고
    • Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli
    • Harlocker, S. L., Bergstrom, L. & Inouye, M. (1995). Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J. Biol. Chem. 270, 26849-26856.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26849-26856
    • Harlocker, S.L.1    Bergstrom, L.2    Inouye, M.3
  • 25
    • 0029843811 scopus 로고    scopus 로고
    • S as a global regulator in the osmotic control of gene expression in Escherichia coli
    • S as a global regulator in the osmotic control of gene expression in Escherichia coli. Mol. Microbiol. 21, 887-893.
    • (1996) Mol. Microbiol. , vol.21 , pp. 887-893
    • Hengge-Aronis, R.1
  • 26
    • 0000073165 scopus 로고    scopus 로고
    • Regulation of gene expression during entry into stationary phase
    • (Neidhardt, F. C., Curtiss, R., III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M. & Umbarger, H. E., eds), 2nd edit., ASM Press, Washington, DC
    • Hengge-Aronis, R. (1996b). Regulation of gene expression during entry into stationary phase. In Escherichia coli and Salmonella (Neidhardt, F. C., Curtiss, R., III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M. & Umbarger, H. E., eds), 2nd edit., pp. 1497-1512, ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella , pp. 1497-1512
    • Hengge-Aronis, R.1
  • 27
    • 0030907937 scopus 로고    scopus 로고
    • A novel role of ImmE7 in the autoregulatory expression of the ColE7 operon and identification of possible RNase active sites in the crystal structure of dimeric ImmE7
    • Hsieh, S.-Y., Ko, T.-P., Tseng, M.-Y., Ku, W.-Y., Chak, K.-F. & Yuan, H. S. (1997). A novel role of ImmE7 in the autoregulatory expression of the ColE7 operon and identification of possible RNase active sites in the crystal structure of dimeric ImmE7. EMBO J. 16, 1444-1454.
    • (1997) EMBO J. , vol.16 , pp. 1444-1454
    • Hsieh, S.-Y.1    Ko, T.-P.2    Tseng, M.-Y.3    Ku, W.-Y.4    Chak, K.-F.5    Yuan, H.S.6
  • 28
    • 0028030535 scopus 로고
    • Sensing starvation: A homoserine lactone-dependent signaling pathway in Escherichia coli
    • Huisman, G. W. & Kolter, R. (1994). Sensing starvation: a homoserine lactone-dependent signaling pathway in Escherichia coli. Science, 265, 537-539.
    • (1994) Science , vol.265 , pp. 537-539
    • Huisman, G.W.1    Kolter, R.2
  • 29
    • 0019309069 scopus 로고
    • Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain, M., Ichihara, S. & Mizushima, S. (1980). Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J. Biol. Chem. 255, 3707-3712.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 30
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in Gram-negative bacteria
    • Jacobs, C., Frère, J. M. & Normark, S. (1997). Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in Gram-negative bacteria. Cell, 88, 823-832.
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frère, J.M.2    Normark, S.3
  • 31
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M. D., Weil, M. & Raff, M. C. (1997). Programmed cell death in animal development. Cell, 88, 347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 32
    • 0029083946 scopus 로고
    • Programmed cell death in bacteria: Proteic plasmid stabilization systems
    • Jensen, R. B. & Gerdes, K. (1995). Programmed cell death in bacteria: proteic plasmid stabilization systems. Mol. Microbiol. 17, 205-10.
    • (1995) Mol. Microbiol. , vol.17 , pp. 205-210
    • Jensen, R.B.1    Gerdes, K.2
  • 33
    • 0025301088 scopus 로고
    • Transcription of osmB, a gene encoding an Escherichia coli lipoprotein, is regulated by dual signals: Osmotic stress and stationary phase
    • Jung, J. U., Gutierrez, C., Martin, F., Ardourel, M. & Villarejo, M. (1990). Transcription of osmB, a gene encoding an Escherichia coli lipoprotein, is regulated by dual signals: osmotic stress and stationary phase. J. Biol. Chem. 265, 10574-10581.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10574-10581
    • Jung, J.U.1    Gutierrez, C.2    Martin, F.3    Ardourel, M.4    Villarejo, M.5
  • 34
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • Kondejewski, L. H., Farmer, S. W., Wishart, D. S., Kay, C. M., Hancock, R. E. W. & Hodges, R. S. (1996). Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 271, 25261-25268.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 35
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange, R. & Hengge-Aronis, R. (1991). Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol. Microbiol. 5, 49-59.
    • (1991) Mol. Microbiol. , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 36
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic max and c-myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • Lavigne, P., Kondejewski, L. H., Houston, M. E., Jr, Sönnichsen, F. D., Lix, B., Sykes, B. D., Hodges, R. S. & Kay, C. M. (1995). Preferential heterodimeric parallel coiled-coil formation by synthetic max and c-myc leucine zippers: a description of putative electrostatic interactions responsible for the specificity of heterodimerization. J. Mol. Biol. 254, 505-520.
    • (1995) J. Mol. Biol. , vol.254 , pp. 505-520
    • Lavigne, P.1    Kondejewski, L.H.2    Houston M.E., Jr.3    Sönnichsen, F.D.4    Lix, B.5    Sykes, B.D.6    Hodges, R.S.7    Kay, C.M.8
  • 37
    • 0000623780 scopus 로고
    • Regulatory components in Citrobacter freundii ampC beta-lactamase induction
    • Lindberg, F., Westman, L. & Normark, S. (1985). Regulatory components in Citrobacter freundii ampC beta-lactamase induction. Proc. Natl Acad. Sci. USA, 82, 4620-4624.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4620-4624
    • Lindberg, F.1    Westman, L.2    Normark, S.3
  • 38
    • 0026583415 scopus 로고
    • Peptide secondary structure induced by a micellar phospholipidic interface: Proton nmr conformational study of a lipopeptide
    • Macquaire, F., Baleux, F., Giaccobi, E., Huynh-Dinh, T., Neumann, J.-M. & Sanson, A. (1992). Peptide secondary structure induced by a micellar phospholipidic interface: proton nmr conformational study of a lipopeptide. Biochemistry, 31, 2576-2582.
    • (1992) Biochemistry , vol.31 , pp. 2576-2582
    • Macquaire, F.1    Baleux, F.2    Giaccobi, E.3    Huynh-Dinh, T.4    Neumann, J.-M.5    Sanson, A.6
  • 39
    • 0028098223 scopus 로고
    • Dicing with death: Dissecting the components of the apoptosis machinery
    • Martin, S. J., Green, D. R. & Cotter, T. G. (1994). Dicing with death: dissecting the components of the apoptosis machinery. Trends Biochem. Sci. 19, 26-30.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 26-30
    • Martin, S.J.1    Green, D.R.2    Cotter, T.G.3
  • 40
    • 0027522090 scopus 로고
    • ChpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda, Y., Miyakawa, K., Nishimura, Y. & Ohtsubo, E. (1993). chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J. Bacteriol. 175, 6850-6856.
    • (1993) J. Bacteriol. , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 41
    • 0029361842 scopus 로고
    • Relationship of side-chain hydrophobicity and α-helical propensity on the stability of the single stranded amphipathic α-helix
    • Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M. & Hodges, R. S. (1995). Relationship of side-chain hydrophobicity and α-helical propensity on the stability of the single stranded amphipathic α-helix. J. Pept. Sci. 1, 319-329.
    • (1995) J. Pept. Sci. , vol.1 , pp. 319-329
    • Monera, O.D.1    Sereda, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 42
    • 0001615484 scopus 로고
    • Theoretical implications for the evolution of postsegregational killing by bacterial plasmids
    • Mongold, J. A. (1992). Theoretical implications for the evolution of postsegregational killing by bacterial plasmids. Am. Nat. 139, 677-689.
    • (1992) Am. Nat. , vol.139 , pp. 677-689
    • Mongold, J.A.1
  • 45
    • 0024311086 scopus 로고
    • A family of genes encoding a cell-killing function may be conserved in all Gram-negative bacteria
    • Poulsen, L. K., Larsen, N. W., Molin, S. & Andersson, P. (1989). A family of genes encoding a cell-killing function may be conserved in all Gram-negative bacteria. Mol. Microbiol. 3, 1463-1472.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1463-1472
    • Poulsen, L.K.1    Larsen, N.W.2    Molin, S.3    Andersson, P.4
  • 46
    • 0028131766 scopus 로고
    • OmpR mutants specifically defective for transcriptional activation
    • Pratt, L. A. & Silhavy, T. J. (1994). OmpR mutants specifically defective for transcriptional activation. J. Mol. Biol. 243, 579-594.
    • (1994) J. Mol. Biol. , vol.243 , pp. 579-594
    • Pratt, L.A.1    Silhavy, T.J.2
  • 47
    • 0029157823 scopus 로고
    • Identification of base pairs important for OmpR-DNA interaction
    • Pratt, L. A. & Silhavy, T. J. (1995). Identification of base pairs important for OmpR-DNA interaction. Mol. Microbiol. 17, 565-573.
    • (1995) Mol. Microbiol. , vol.17 , pp. 565-573
    • Pratt, L.A.1    Silhavy, T.J.2
  • 48
    • 0028947721 scopus 로고
    • Kid, a small protein of the parD stability system of plasmid R1, is an inhibitor of DNa replication acting on the initiation of DNa synthesis
    • Ruiz-Echevarria, M. J., Gimenez-Gallego, G., Sabariegos-Jareno, R. & Diaz-Orejas, R. (1995). Kid, a small protein of the parD stability system of plasmid R1, is an inhibitor of DNA replication acting on the initiation of DNA synthesis. J. Mol. Biol. 247, 568-577.
    • (1995) J. Mol. Biol. , vol.247 , pp. 568-577
    • Ruiz-Echevarria, M.J.1    Gimenez-Gallego, G.2    Sabariegos-Jareno, R.3    Diaz-Orejas, R.4
  • 50
    • 0029000609 scopus 로고
    • Modification of bacterial lipoproteins
    • Sankaran, K., Gupta, S. D. & Wu, H. C. (1995). Modification of bacterial lipoproteins. Methods Enzymol. 250, 683-697.
    • (1995) Methods Enzymol. , vol.250 , pp. 683-697
    • Sankaran, K.1    Gupta, S.D.2    Wu, H.C.3
  • 51
    • 0030787581 scopus 로고    scopus 로고
    • Functional interactions between homologous conditional killer systems of plasmid and chromosomal origin
    • Santos-Sierra, S., Giraldo, R. & Diaz-Orejas, R. (1997). Functional interactions between homologous conditional killer systems of plasmid and chromosomal origin. FEMS Micriobiol. Letters, 152, 51-56.
    • (1997) FEMS Micriobiol. Letters , vol.152 , pp. 51-56
    • Santos-Sierra, S.1    Giraldo, R.2    Diaz-Orejas, R.3
  • 52
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 53
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer, J. & Edmundson, A. B. (1967). Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J. 7, 121-135.
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, J.1    Edmundson, A.B.2
  • 54
    • 0028450103 scopus 로고
    • Bacterial altruism?
    • Shub, D. A. (1994). Bacterial altruism? Curr. Biol. 4, 555-556.
    • (1994) Curr. Biol. , vol.4 , pp. 555-556
    • Shub, D.A.1
  • 55
    • 0028953424 scopus 로고
    • Phage-exclusion enzymes: A bonanza of biochemical and cell biology reagents?
    • Snyder, L. (1995). Phage-exclusion enzymes: a bonanza of biochemical and cell biology reagents? Mol. Microbiol. 15, 415-420.
    • (1995) Mol. Microbiol. , vol.15 , pp. 415-420
    • Snyder, L.1
  • 56
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry, 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 57
    • 0026708136 scopus 로고
    • A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- And P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4
    • Strack, B., Lessl, M., Calendar, R. & Lanka, E. (1992). A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- and P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4. J. Biol. Chem. 267, 13062-13072.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13062-13072
    • Strack, B.1    Lessl, M.2    Calendar, R.3    Lanka, E.4
  • 58
    • 0027369494 scopus 로고
    • Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes: Cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability
    • Tytler, E. M., Segrest, J. P., Epand, R. M., Nie, Q., Epand, R. F., Mishra, V. K., Venkatachalapathi, Y. V. & Anantharamaiah, G. M. (1993). Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes: cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability. J. Biol. Chem. 268, 22112-22118.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22112-22118
    • Tytler, E.M.1    Segrest, J.P.2    Epand, R.M.3    Nie, Q.4    Epand, R.F.5    Mishra, V.K.6    Venkatachalapathi, Y.V.7    Anantharamaiah, G.M.8
  • 59
    • 84982610130 scopus 로고
    • Bacteriocin release proteins: Mode of action, structure, and biotechnological application
    • van der Wal, F. J., Luirink, J. & Oudega, B. (1995). Bacteriocin release proteins: mode of action, structure, and biotechnological application. FEMS Microbiol. Rev. 17, 381-399.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 381-399
    • Van Der Wal, F.J.1    Luirink, J.2    Oudega, B.3
  • 62
    • 0028353294 scopus 로고
    • SEQSEE: A comprehensive suite for protein sequence analysis
    • Wishart, D. S., Boyko, R. F., Willard, L., Richards, F. M. & Sykes, B. D. (1994). SEQSEE: a comprehensive suite for protein sequence analysis. CABIOS, 10, 121-132.
    • (1994) CABIOS , vol.10 , pp. 121-132
    • Wishart, D.S.1    Boyko, R.F.2    Willard, L.3    Richards, F.M.4    Sykes, B.D.5
  • 63
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K., Yu, F. & Inouye, M. (1988). A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell, 53, 423-32.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 64
    • 0028963606 scopus 로고
    • Programmed cell death in bacterial populations
    • Yarmolinsky, M. B. (1995). Programmed cell death in bacterial populations. Science, 267, 836-837.
    • (1995) Science , vol.267 , pp. 836-837
    • Yarmolinsky, M.B.1
  • 65
    • 0028120890 scopus 로고
    • Translational elongation factor Tu cleaved by a phage-exclusion system
    • Yu, Y. T. & Snyder, L. (1994). Translational elongation factor Tu cleaved by a phage-exclusion system. Proc. Natl Acad. Sci. USA, 91, 802-806.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 802-806
    • Yu, Y.T.1    Snyder, L.2
  • 67
    • 0030602818 scopus 로고    scopus 로고
    • Gasping for life in stationary phase
    • Zambrano, M. M. & Kolter, R. (1996). Gasping for life in stationary phase. Cell, 86, 181-184.
    • (1996) Cell , vol.86 , pp. 181-184
    • Zambrano, M.M.1    Kolter, R.2
  • 68
    • 0027510647 scopus 로고
    • Microbial competition: Escherichia coli mutants that take over stationary phase cultures
    • Zambrano, M. M., Siegele, D. A., Almirón, M., Tormo, A. & Kolter, R. (1993). Microbial competition: Escherichia coli mutants that take over stationary phase cultures. Science, 259, 1757-1760.
    • (1993) Science , vol.259 , pp. 1757-1760
    • Zambrano, M.M.1    Siegele, D.A.2    Almirón, M.3    Tormo, A.4    Kolter, R.5
  • 69
    • 0027995873 scopus 로고
    • α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix
    • Zhou, N. E., Monera, O. D., Kay, C. M. & Hodges, R. S. (1994). α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix. Protein Pept. Letters, 1, 114-119.
    • (1994) Protein Pept. Letters , vol.1 , pp. 114-119
    • Zhou, N.E.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.