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Volumn 187, Issue 13, 2005, Pages 4552-4561

Characterization of six lipoproteins in the σe regulon

Author keywords

[No Author keywords available]

Indexed keywords

BACTERICIDAL PERMEABILITY INCREASING PROTEIN; CHAPERONE; DODECYL SULFATE SODIUM; LIPOPROTEIN; OUTER MEMBRANE PROTEIN; RIFAMPICIN; ENZYME INHIBITOR; ESCHERICHIA COLI PROTEIN; SIGMA E FACTOR; SIGMA FACTOR; SIGMA-E FACTOR; SURFACTANT; TRANSCRIPTION FACTOR; YFIO PROTEIN, E COLI;

EID: 17444392068     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.13.4552-4561.2005     Document Type: Article
Times cited : (127)

References (55)
  • 1
    • 0033568606 scopus 로고    scopus 로고
    • e dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • E dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev. 13:2449-2461.
    • (1999) Genes Dev. , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 3
    • 0009002119 scopus 로고    scopus 로고
    • Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide
    • Barker, H. C., N. Kinsella, A. Jaspe, T. Friedrich, and C. D. O'Connor. 2000. Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide. Mol. Microbiol. 35:1518-1529.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1518-1529
    • Barker, H.C.1    Kinsella, N.2    Jaspe, A.3    Friedrich, T.4    O'Connor, C.D.5
  • 4
    • 0030761825 scopus 로고    scopus 로고
    • A role for rseC, a gene in the rpoE cluster, in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J., L. E. Connolly, A. De Las Peñas, and D. M. Downs. 1997. A role for rseC, a gene in the rpoE cluster, in thiamine synthesis in Salmonella typhimurium. J. Bacteriol. 179:6504-6508.
    • (1997) J. Bacteriol. , vol.179 , pp. 6504-6508
    • Beck, B.J.1    Connolly, L.E.2    De Las Peñas, A.3    Downs, D.M.4
  • 5
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., R. Maier, H. de Cock, F. X. Schmid, and C. A. Gross. 2001. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20:285-294.
    • (2001) EMBO J. , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 7
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann, H., and A. Pluckthun. 1998. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat. Biotechnol. 16:376-380.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 8
    • 0025953663 scopus 로고
    • A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome
    • Bouvier, J., A. P. Pugsley, and P. Stragier. 1991. A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome. J. Bacteriol. 173:5523-5531.
    • (1991) J. Bacteriol. , vol.173 , pp. 5523-5531
    • Bouvier, J.1    Pugsley, A.P.2    Stragier, P.3
  • 9
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R., and U. Henning. 1996. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19:1287-1294.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 10
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P., and W. Wackernagel. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein
    • De Cock, H., U. Schafer, M. Potgeter, R. Demel, M. Muller, and J. Tommassen. 1999. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259:96-103.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • De Cock, H.1    Schafer, U.2    Potgeter, M.3    Demel, R.4    Muller, M.5    Tommassen, J.6
  • 14
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh, T., I. T. Paulsen, and M. H. Saier, Jr. 1994. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J. Bacteriol. 176:3825-3831.
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr., M.H.3
  • 15
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • Eggert, U. S., N. Ruiz, B. V. Falcone, A. A. Branstrom, R. C. Goldman, T. J. Silhavy, and D. Kahne. 2001. Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin. Science 294:361-364.
    • (2001) Science , vol.294 , pp. 361-364
    • Eggert, U.S.1    Ruiz, N.2    Falcone, B.V.3    Branstrom, A.A.4    Goldman, R.C.5    Silhavy, T.J.6    Kahne, D.7
  • 16
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle, I., K. Gabriel, P. Beech, R. Waller, and T. Lithgow. 2004. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 164:19-24.
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 17
    • 0025769947 scopus 로고
    • The mdoA locus of Escherichia coli consists of an operon under osmotic control
    • Lacroix, J. M., I. Loubens, M. Tempete, B. Menichi, and J. P. Bohin. 1991. The mdoA locus of Escherichia coli consists of an operon under osmotic control. Mol. Microbiol. 5:1745-1753.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1745-1753
    • Lacroix, J.M.1    Loubens, I.2    Tempete, M.3    Menichi, B.4    Bohin, J.P.5
  • 18
    • 0034944420 scopus 로고    scopus 로고
    • The Tol-Pal proteins of the Escherichia coli cell envelope: An energized system required for outer membrane integrity?
    • Lloubes, R., E. Cascales, A. Walburger, E. Bouveret, C. Lazdunski, A. Bernadac, and L. Journet. 2001. The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity? Res. Microbiol. 152:523-529.
    • (2001) Res. Microbiol. , vol.152 , pp. 523-529
    • Lloubes, R.1    Cascales, E.2    Walburger, A.3    Bouveret, E.4    Lazdunski, C.5    Bernadac, A.6    Journet, L.7
  • 19
    • 0026686805 scopus 로고
    • Emr, an Escherichia coli locus for multidrug resistance
    • Lomovskaya, O., and K. Lewis. 1992. Emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. USA 89:8938-8942.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 20
    • 0028999706 scopus 로고
    • EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB
    • Lomovskaya, O., K. Lewis, and A. Matin. 1995. EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB. J. Bacteriol. 177:2328-2334.
    • (1995) J. Bacteriol. , vol.177 , pp. 2328-2334
    • Lomovskaya, O.1    Lewis, K.2    Matin, A.3
  • 21
    • 0027508337 scopus 로고
    • Molecular cloning and characterization of acrA and acrE genes of Escherichia coli
    • Ma, D., D. N. Cook, M. Alberti, N. G. Pon, H. Nikaido, and J. E. Hearst. 1993. Molecular cloning and characterization of acrA and acrE genes of Escherichia coli. J. Bacteriol. 175:6299-6313.
    • (1993) J. Bacteriol. , vol.175 , pp. 6299-6313
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 22
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama, S., T. Tajima, and H. Tokuda. 1995. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J. 14:3365-3372.
    • (1995) EMBO J. , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 23
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM). involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama, S., N. Yokota, and H. Tokuda. 1997. A novel outer membrane lipoprotein, LolB (HemM). involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J. 16:6947-6955.
    • (1997) EMBO J. , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 24
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 25
    • 0030462757 scopus 로고    scopus 로고
    • Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
    • Missiakas, D., F. Schwager, J. M. Betton, C. Georgopoulos, and S. Raina. 1996. Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15:6899-6909.
    • (1996) EMBO J. , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.M.3    Georgopoulos, C.4    Raina, S.5
  • 26
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • Miyadai, H., K. Tanaka-Masuda, S. I. Matsuyama, and H. Tokuda. 2004. Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J. Biol. Chem. 279:39807-39813.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.I.3    Tokuda, H.4
  • 27
    • 0035850777 scopus 로고    scopus 로고
    • Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB
    • Miyamoto, A., S. Matsuyama, and H. Tokuda. 2001. Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB. Biochem. Biophys. Res. Commun. 287: 1125-1128.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 1125-1128
    • Miyamoto, A.1    Matsuyama, S.2    Tokuda, H.3
  • 28
    • 0031924072 scopus 로고    scopus 로고
    • Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli
    • Murphy, K. C. 1998. Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli. J. Bacteriol. 180:2063-2071.
    • (1998) J. Bacteriol. , vol.180 , pp. 2063-2071
    • Murphy, K.C.1
  • 29
    • 4544384204 scopus 로고    scopus 로고
    • Lipoprotein trafficking in Escherichia coli
    • Narita, S., S. Matsuyama, and H. Tokuda. 2004. Lipoprotein trafficking in Escherichia coli. Arch. Microbiol. 182:1-6.
    • (2004) Arch. Microbiol. , vol.182 , pp. 1-6
    • Narita, S.1    Matsuyama, S.2    Tokuda, H.3
  • 30
    • 0036175948 scopus 로고    scopus 로고
    • Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane
    • Narita, S., K. Tanaka, S. Matsuyama, and H. Tokuda. 2002. Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane. J. Bacteriol. 184:1417-1422.
    • (2002) J. Bacteriol. , vol.184 , pp. 1417-1422
    • Narita, S.1    Tanaka, K.2    Matsuyama, S.3    Tokuda, H.4
  • 31
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Nikaido, H. 1996. Outer membrane, p. 29-47. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 29-47
    • Nikaido, H.1
  • 32
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • Nikaido, H. 1994. Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269:3905-3908.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 34
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • Raivio, T. L., and T. J. Silhavy. 2001. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:591-624.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 36
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello, A. E., J. R. Harper, and T. J. Silhavy. 2001. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 183:6794-6800.
    • (2001) J. Bacteriol. , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 38
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière, P. G., and C. A. Gross. 1996. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:3170-3182.
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouvière, P.G.1    Gross, C.A.2
  • 39
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • Ruiz, N., B. Falcone, D. Kahne, and T. J. Silhavy. 2005. Chemical conditionality: a genetic strategy to probe organelle assembly. Cell 121:307-317.
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 40
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., and H. C. Wu. 1994. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269:19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 42
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., A. Beil, and M. Ehrmann. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 43
    • 0032515174 scopus 로고    scopus 로고
    • Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins
    • Tajima, T., N. Yokota, S. Matsuyama, and H. Tokuda. 1998. Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins. FEBS Lett. 439:51-54.
    • (1998) FEBS Lett. , vol.439 , pp. 51-54
    • Tajima, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 44
    • 0034750231 scopus 로고    scopus 로고
    • Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm
    • Tanaka, K., S. I. Matsuyama, and H. Tokuda. 2001. Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm. J. Bacteriol. 183:6538-6542.
    • (2001) J. Bacteriol. , vol.183 , pp. 6538-6542
    • Tanaka, K.1    Matsuyama, S.I.2    Tokuda, H.3
  • 45
    • 0036784072 scopus 로고    scopus 로고
    • Multidrug pump inhibitors uncover remarkable activity of plant antimicrobials
    • Tegos, G., F. R. Stermitz, O. Lomovskaya, and K. Lewis. 2002. Multidrug pump inhibitors uncover remarkable activity of plant antimicrobials. Antimicrob. Agents Chemother. 46:3133-3141.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3133-3141
    • Tegos, G.1    Stermitz, F.R.2    Lomovskaya, O.3    Lewis, K.4
  • 46
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., M. P. Bos, J. Geurtsen, M. Mols, and J. Tommassen. 2003. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 47
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh, N. P., B. M. Alba, B. Bose, C. A. Gross, and R. T. Sauer. 2003. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113:61-71.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 48
    • 0043069635 scopus 로고    scopus 로고
    • Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): Structure, function and regulation in host defence against Gram-negative bacteria
    • Weiss, J. 2003. Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure, function and regulation in host defence against Gram-negative bacteria. Biochem. Soc. Trans. 31: 785-790.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 785-790
    • Weiss, J.1
  • 49
    • 0000587078 scopus 로고    scopus 로고
    • Biosynthesis of lipoproteins
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Wu, H. C. 1996. Biosynthesis of lipoproteins, p. 1005-1014. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 1005-1014
    • Wu, H.C.1
  • 50
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., J. Malinverni, N. Ruiz, S. Kim, T. J. Silhavy, and D. Kahne. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 51
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi, T., K. Masuda, S. Narita, S. Matsuyama, and H. Tokuda. 2000. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat. Cell Biol. 2:212-218.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 52
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K., F. Yu, and M. Inouye. 1988. A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell 53:423-432.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 53
    • 0017665289 scopus 로고
    • Genetic characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein
    • Yem, D. W., and H. C. Wu. 1977. Genetic characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein. J. Bacteriol. 131:759-764.
    • (1977) J. Bacteriol. , vol.131 , pp. 759-764
    • Yem, D.W.1    Wu, H.C.2
  • 54
    • 0017836107 scopus 로고
    • Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein
    • Yem, D. W., and H. C. Wu. 1978. Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein. J. Bacteriol. 133:1419-1426.
    • (1978) J. Bacteriol. , vol.133 , pp. 1419-1426
    • Yem, D.W.1    Wu, H.C.2
  • 55
    • 0033118799 scopus 로고    scopus 로고
    • Regulation of the heat-shock response
    • Yura, T., and K. Nakahigashi. 1999. Regulation of the heat-shock response. Curr. Opin. Microbiol. 2:153-158.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 153-158
    • Yura, T.1    Nakahigashi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.