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Volumn 57, Issue 4, 2005, Pages 900-912

The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; BACTERIAL PROTEIN; LIPID A; MAGNESIUM ION; PROTEIN PALMITOYLTRANSFERASE PAGP; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 23744436588     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04711.x     Document Type: Short Survey
Times cited : (140)

References (101)
  • 1
    • 4444328639 scopus 로고    scopus 로고
    • Lactose permease as a paradigm for membrane transport proteins
    • Abramson, J., Iwata, S., and Kaback, H.R. (2004) Lactose permease as a paradigm for membrane transport proteins (Review). Mol Membr Biol 21: 227-236.
    • (2004) Mol Membr Biol , vol.21 , pp. 227-236
    • Abramson, J.1    Iwata, S.2    Kaback, H.R.3
  • 2
    • 4143131241 scopus 로고    scopus 로고
    • A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin
    • Ahn, V.E., Lo, E.I., Engel, C.K., Chen, L., Hwang, P.M., Kay, L.E., et al. (2004) A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin. EMBO J 23:2931-2941.
    • (2004) EMBO J , vol.23 , pp. 2931-2941
    • Ahn, V.E.1    Lo, E.I.2    Engel, C.K.3    Chen, L.4    Hwang, P.M.5    Kay, L.E.6
  • 3
    • 2442563573 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli sigma E-dependent envelope stress response
    • Alba, B.M., and Gross, C.A. (2004) Regulation of the Escherichia coli sigma E-dependent envelope stress response. Mol Microbiol 52: 613-619.
    • (2004) Mol Microbiol , vol.52 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 4
    • 0343851592 scopus 로고    scopus 로고
    • Novel variation of lipid A structures in strains of different Yersinia species
    • Aussel, L., Therisod, H., Karibian, D., Perry, M.B., Bruneteau, M., and Caroff, M. (2000) Novel variation of lipid A structures in strains of different Yersinia species. FEBS Lett 465: 87-92.
    • (2000) FEBS Lett , vol.465 , pp. 87-92
    • Aussel, L.1    Therisod, H.2    Karibian, D.3    Perry, M.B.4    Bruneteau, M.5    Caroff, M.6
  • 5
    • 0141818919 scopus 로고    scopus 로고
    • Regulation of Salmonella typhimurium virulence gene expression by cationic antimicrobial peptides
    • Bader, M.W., Navarre, W.W., Shiau, W., Nikaido, H., Frye, J.G., McClelland, M., et al. (2003) Regulation of Salmonella typhimurium virulence gene expression by cationic antimicrobial peptides. Mol Microbiol 50: 219-230.
    • (2003) Mol Microbiol , vol.50 , pp. 219-230
    • Bader, M.W.1    Navarre, W.W.2    Shiau, W.3    Nikaido, H.4    Frye, J.G.5    McClelland, M.6
  • 6
    • 0028148530 scopus 로고
    • Further characterization of the PhoP regulon: Identification of new PhoP-activated virulence loci
    • Beiden, W.J., and Miller, S.I. (1994) Further characterization of the PhoP regulon: identification of new PhoP-activated virulence loci. Infect Immun 62: 5095-5101.
    • (1994) Infect Immun , vol.62 , pp. 5095-5101
    • Beiden, W.J.1    Miller, S.I.2
  • 7
    • 0034684162 scopus 로고    scopus 로고
    • The bacterial lipocalins
    • Bishop, R.E. (2000) The bacterial lipocalins. Biochim Biophys Acta 1482: 73-83.
    • (2000) Biochim Biophys Acta , vol.1482 , pp. 73-83
    • Bishop, R.E.1
  • 8
    • 16544370292 scopus 로고    scopus 로고
    • Fundamentals of endotoxin structure and function
    • Bishop, R.E. (2005) Fundamentals of endotoxin structure and function. Contrib Microbiol 12: 1-27.
    • (2005) Contrib Microbiol , vol.12 , pp. 1-27
    • Bishop, R.E.1
  • 9
    • 33645201918 scopus 로고    scopus 로고
    • Purified his6-PagP involved in antimicrobial peptide resistance catalyzes the acylation of numerous alcohols
    • Vol. Abst. 2290. Toronto, ON, Canada
    • Bishop, R.E., and Raetz, C.R. (2000) Purified his6-PagP involved in antimicrobial peptide resistance catalyzes the acylation of numerous alcohols. In Fortieth Interscience Conference on Antimicrobial Agents and Chemotherapy. Vol. Abst. 2290. Toronto, ON, Canada, pp. 133.
    • (2000) Fortieth Interscience Conference on Antimicrobial Agents and Chemotherapy , pp. 133
    • Bishop, R.E.1    Raetz, C.R.2
  • 10
    • 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, LS., Holtje, J.V., and 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    Holtje, J.V.4    Weiner, J.H.5
  • 11
    • 0032563108 scopus 로고    scopus 로고
    • The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death
    • Bishop, R.E., Leskiw, B.K., Hodges, R.S., Kay, C.M., and Weiner, J.H. (1998) The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death. J Mol Biol 280: 583-596.
    • (1998) J Mol Biol , vol.280 , pp. 583-596
    • Bishop, R.E.1    Leskiw, B.K.2    Hodges, R.S.3    Kay, C.M.4    Weiner, J.H.5
  • 12
    • 0034596969 scopus 로고    scopus 로고
    • Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria
    • Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I., and Raetz, C.R. (2000) Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J 19: 5071-5080.
    • (2000) EMBO J , vol.19 , pp. 5071-5080
    • Bishop, R.E.1    Gibbons, H.S.2    Guina, T.3    Trent, M.S.4    Miller, S.I.5    Raetz, C.R.6
  • 13
    • 8844219773 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M.P., and Tommassen, J. (2004) Biogenesis of the Gram-negative bacterial outer membrane. Curr Opin Microbiol 7: 610-616.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 610-616
    • Bos, M.P.1    Tommassen, J.2
  • 14
    • 3042554408 scopus 로고    scopus 로고
    • Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface
    • Bos, M.P., Tefsen, B., Geurtsen, J., and Tommassen, J. (2004) Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface. Proc Natl Acad Sci USA 101: 9417-9422.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9417-9422
    • Bos, M.P.1    Tefsen, B.2    Geurtsen, J.3    Tommassen, J.4
  • 15
    • 0036046150 scopus 로고    scopus 로고
    • Imp/OstA is required for cell envelope biogenesis in Escherichia coli
    • Braun, M., and Silhavy, T.J. (2002) Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol Microbiol 45: 1289-1302.
    • (2002) Mol Microbiol , vol.45 , pp. 1289-1302
    • Braun, M.1    Silhavy, T.J.2
  • 16
    • 0023654461 scopus 로고
    • Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X
    • Brozek, K.A., Bulawa, C.E., and Raetz, C.R. (1987) Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X. J Biol Chem 262: 5170-5179.
    • (1987) J Biol Chem , vol.262 , pp. 5170-5179
    • Brozek, K.A.1    Bulawa, C.E.2    Raetz, C.R.3
  • 17
    • 4644293305 scopus 로고    scopus 로고
    • Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis
    • Chain, P.S., Carniel, E., Larimer, F.W., Lamerdin, J., Stoutland, P.O., Regala, W.M., et al. (2004) Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis. Proc Natl Acad Sci USA 101: 13826-13831.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13826-13831
    • Chain, P.S.1    Carniel, E.2    Larimer, F.W.3    Lamerdin, J.4    Stoutland, P.O.5    Regala, W.M.6
  • 18
    • 0242573103 scopus 로고    scopus 로고
    • Multidrug resistance ABC transporters
    • Chang, G. (2003) Multidrug resistance ABC transporters. FEBS Lett 555: 102-105.
    • (2003) FEBS Lett , vol.555 , pp. 102-105
    • Chang, G.1
  • 19
    • 0031580211 scopus 로고    scopus 로고
    • Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12
    • de Cock, H., Struyve, M., Kleerebezem, M., van der Krift, T., and Tommassen, J. (1997) Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12. J Mol Biol 269: 473-478.
    • (1997) J Mol Biol , vol.269 , pp. 473-478
    • De Cock, H.1    Struyve, M.2    Kleerebezem, M.3    Van Der Krift, T.4    Tommassen, J.5
  • 20
    • 1342346634 scopus 로고    scopus 로고
    • The PhoP-PhoQ two-component regulatory system of Photorhabdus luminescens is essential for virulence in insects
    • Derzelle, S., Turlin, E., Duchaud, E., Pages, S., Kunst, F., Givaudan, A., and Danchin, A. (2004) The PhoP-PhoQ two-component regulatory system of Photorhabdus luminescens is essential for virulence in insects. J Bacteriol 186: 1270-1279.
    • (2004) J Bacteriol , vol.186 , pp. 1270-1279
    • Derzelle, S.1    Turlin, E.2    Duchaud, E.3    Pages, S.4    Kunst, F.5    Givaudan, A.6    Danchin, A.7
  • 21
    • 0037184103 scopus 로고    scopus 로고
    • ATPase activity of the MsbA lipid flippase of Escherichia coli
    • Doerrler, W.T., and Raetz, C.R. (2002) ATPase activity of the MsbA lipid flippase of Escherichia coli. J Biol Chem 277: 36697-36705.
    • (2002) J Biol Chem , vol.277 , pp. 36697-36705
    • Doerrler, W.T.1    Raetz, C.R.2
  • 22
    • 0035853703 scopus 로고    scopus 로고
    • An Escherichia coli mutant defective in lipid export
    • Doerrler, W.T., Reedy, M.C., and Raetz, C.R. (2001) An Escherichia coli mutant defective in lipid export. J Biol Chem 276: 11461-11464.
    • (2001) J Biol Chem , vol.276 , pp. 11461-11464
    • Doerrler, W.T.1    Reedy, M.C.2    Raetz, C.R.3
  • 23
    • 7244248683 scopus 로고    scopus 로고
    • MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli
    • Doerrler, W.T., Gibbons, H.S., and Raetz, C.R. (2004) MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli. J Biol Chem 279: 45102-45109.
    • (2004) J Biol Chem , vol.279 , pp. 45102-45109
    • Doerrler, W.T.1    Gibbons, H.S.2    Raetz, C.R.3
  • 24
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan, W. (1997) Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu Rev Biochem 66: 199-232.
    • (1997) Annu Rev Biochem , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 25
    • 2342501446 scopus 로고    scopus 로고
    • Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli
    • Eguchi, Y., Okada, T., Minagawa, S., Oshima, T., Mori, H., Yamamoto, K., et al. (2004) Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli. J Bacteriol 186: 3006-3014.
    • (2004) J Bacteriol , vol.186 , pp. 3006-3014
    • Eguchi, Y.1    Okada, T.2    Minagawa, S.3    Oshima, T.4    Mori, H.5    Yamamoto, K.6
  • 26
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand, R.M., Shai, Y., Segrest, J.P., and 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
  • 27
    • 0033584935 scopus 로고    scopus 로고
    • Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa
    • Ernst, R.K., Yi, E.G., Quo, L., Lim, K.B., Burns, J.L., Hackett, M., and Miller, S.I. (1999) Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa. Science 286: 1561-1565.
    • (1999) Science , vol.286 , pp. 1561-1565
    • Ernst, R.K.1    Yi, E.G.2    Quo, L.3    Lim, K.B.4    Burns, J.L.5    Hackett, M.6    Miller, S.I.7
  • 28
    • 0024446808 scopus 로고
    • Induction of tumor necrosis factor-alpha release by lipopolysaccharide and defined lipopolysaccharide partial structures
    • Feist, W., Ulmer, A.J., Musehold, J., Brade, H., Kusumoto, S., and Flad, H.D. (1989) Induction of tumor necrosis factor-alpha release by lipopolysaccharide and defined lipopolysaccharide partial structures. Immunobiology 179: 293-307.
    • (1989) Immunobiology , vol.179 , pp. 293-307
    • Feist, W.1    Ulmer, A.J.2    Musehold, J.3    Brade, H.4    Kusumoto, S.5    Flad, H.D.6
  • 29
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes, J.R., and Gros, P. (2001) Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol 9: 397-403.
    • (2001) Trends Microbiol , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 30
    • 0035830602 scopus 로고    scopus 로고
    • Physico-chemical analysis of lipid A fractions of lipopolysaccharide from Erwinia carotovora in relation to bioactivity
    • Fukuoka, S., Brandenburg, K., Muller, M., Lindner, B., Koch, M.H., and Seydel, U. (2001) Physico-chemical analysis of lipid A fractions of lipopolysaccharide from Erwinia carotovora in relation to bioactivity. Biochim Biophys Acta 1510: 185-197.
    • (2001) Biochim Biophys Acta , vol.1510 , pp. 185-197
    • Fukuoka, S.1    Brandenburg, K.2    Muller, M.3    Lindner, B.4    Koch, M.H.5    Seydel, U.6
  • 31
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84: 165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 32
    • 14844316639 scopus 로고    scopus 로고
    • Dissemination of lipid A deacylases (PagL) among gram-negative bacteria: Identification of active-site histidine and serine residues
    • Geurtsen, J., Steeghs, L., Hove, J.T., Ley, P.V., and Tommassen, J. (2005) Dissemination of lipid A deacylases (PagL) among gram-negative bacteria: identification of active-site histidine and serine residues. J Biol Chem 280: 8248-8259.
    • (2005) J Biol Chem , vol.280 , pp. 8248-8259
    • Geurtsen, J.1    Steeghs, L.2    Hove, J.T.3    Ley, P.V.4    Tommassen, J.5
  • 34
    • 13144306075 scopus 로고    scopus 로고
    • 2+ and pH in the modification of Salmonella lipid A after endocytosis by macrophage tumour cells
    • 2+ and pH in the modification of Salmonella lipid A after endocytosis by macrophage tumour cells. Mol Microbiol 55: 425-440.
    • (2005) Mol Microbiol , vol.55 , pp. 425-440
    • Gibbons, H.S.1    Kalb, S.R.2    Cotter, R.J.3    Raetz, C.R.4
  • 35
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman, E.A. (2001) The pleiotropic two-component regulatory system PhoP-PhoQ. J Bacteriol 183: 1835-1842.
    • (2001) J Bacteriol , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 36
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina, T., Yi, E.G., Wang, H., Hackett, M., and Miller, S.I. (2000) A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides. J Bacteriol 182: 4077-4086.
    • (2000) J Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.G.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 37
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Quo, L., Lim, K.B., Gunn, U.S., Bainbridge, B., Darveau, R.P., Hackett, M., and Miller, S.I. (1997) Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276: 250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Quo, L.1    Lim, K.B.2    Gunn, U.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 38
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Quo, L., Lim, K.B., Poduje, C.M., Daniel, M., Gunn, U.S., Hackett, M., and Miller, S.I. (1998) Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 95: 189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Quo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, U.S.5    Hackett, M.6    Miller, S.I.7
  • 40
    • 0018347990 scopus 로고
    • Effect of ethylenedi-aminetetraacetate on phospholipids and outer membrane function in Escherichia coli
    • Hardaway, K.L., and Buller, C.S. (1979) Effect of ethylenedi- aminetetraacetate on phospholipids and outer membrane function in Escherichia coli. J Bacteriol 137: 62-68.
    • (1979) J Bacteriol , vol.137 , pp. 62-68
    • Hardaway, K.L.1    Buller, C.S.2
  • 41
    • 3142713223 scopus 로고    scopus 로고
    • Inhibition of endotoxin response by synthetic TLR4 antagonists
    • Hawkins, L.D., Christ, W.J., and Rossignol, D.P. (2004) Inhibition of endotoxin response by synthetic TLR4 antagonists. Curr Top Med Chem 4: 1147-1171.
    • (2004) Curr Top Med Chem , vol.4 , pp. 1147-1171
    • Hawkins, L.D.1    Christ, W.J.2    Rossignol, D.P.3
  • 42
    • 0024618579 scopus 로고
    • Uptake and acylation of 2-acyl-lysophospholipids by Escherichia coli
    • Hsu, L., Jackowski, S., and Rock, C.O. (1989) Uptake and acylation of 2-acyl-lysophospholipids by Escherichia coli. J Bacteriol 171: 1203-1205.
    • (1989) J Bacteriol , vol.171 , pp. 1203-1205
    • Hsu, L.1    Jackowski, S.2    Rock, C.O.3
  • 43
    • 16244421653 scopus 로고    scopus 로고
    • Solution structure and dynamics of integral membrane proteins by NMR: A case study involving the enzyme PagP
    • Hwang, P.M., and Kay, L.E. (2005) Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP. Methods Enzymol 394: 335-350.
    • (2005) Methods Enzymol , vol.394 , pp. 335-350
    • Hwang, P.M.1    Kay, L.E.2
  • 45
    • 3042707182 scopus 로고    scopus 로고
    • The integral membrane enzyme PagP alternates between two dynamically distinct states
    • Hwang, P.M., Bishop, R.E., and Kay, L.E. (2004) The integral membrane enzyme PagP alternates between two dynamically distinct states. Proc Natl Acad Sci USA 101: 9618-9623.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9618-9623
    • Hwang, P.M.1    Bishop, R.E.2    Kay, L.E.3
  • 46
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune responses
    • Iwasaki, A., and Medzhitov, R. (2004) Toll-like receptor control of the adaptive immune responses. Nat Immunol 5: 987-995.
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 47
    • 0036449405 scopus 로고    scopus 로고
    • Structural and biological characterization of highly purified hepta-acyl lipid A present in the lipopolysaccharide of the Salmonella enterica sv. Minnesota Re deep rough mutant strain R595
    • Janusch, H., Brecker, L., Lindner, B., Alexander, C., Gronow, S., Heine, H., et al. (2002) Structural and biological characterization of highly purified hepta-acyl lipid A present in the lipopolysaccharide of the Salmonella enterica sv. Minnesota Re deep rough mutant strain R595. J Endotoxin Res 8: 343-356.
    • (2002) J Endotoxin Res , vol.8 , pp. 343-356
    • Janusch, H.1    Brecker, L.2    Lindner, B.3    Alexander, C.4    Gronow, S.5    Heine, H.6
  • 50
    • 0017660232 scopus 로고
    • Translocation of phospholipids between the outer and inner membranes of Salmonella typhimurium
    • Jones, N.C., and Osborn, M.J. (1977) Translocation of phospholipids between the outer and inner membranes of Salmonella typhimurium. J Biol Chem 252: 7405-7412.
    • (1977) J Biol Chem , vol.252 , pp. 7405-7412
    • Jones, N.C.1    Osborn, M.J.2
  • 51
    • 0017188213 scopus 로고
    • Outer membrane of Salmonella typhimurium: Accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium
    • Kamio, Y., and Nikaido, H. (1976) Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium. Biochemistry 15: 2561-2570.
    • (1976) Biochemistry , vol.15 , pp. 2561-2570
    • Kamio, Y.1    Nikaido, H.2
  • 52
    • 0141891335 scopus 로고    scopus 로고
    • Expression cloning and biochemical characterization of a Rhizobium leguminosarum lipid A 1-phosphatase
    • Karbarz, MJ., Kalb, S.R., Cotter, R.J., and Raetz, C.R. (2003) Expression cloning and biochemical characterization of a Rhizobium leguminosarum lipid A 1-phosphatase. J Biol Chem 278: 39269-39279.
    • (2003) J Biol Chem , vol.278 , pp. 39269-39279
    • Karbarz, M.J.1    Kalb, S.R.2    Cotter, R.J.3    Raetz, C.R.4
  • 53
    • 2442544458 scopus 로고    scopus 로고
    • 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through toll-like receptor 4
    • Kawasaki, K., Ernst, R.K., and Miller, S.I. (2004) 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through toll-like receptor 4. J Biol Chem 279: 20044-20048.
    • (2004) J Biol Chem , vol.279 , pp. 20044-20048
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 54
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim, M., Carman, C.V., and Springer, T.A. (2003) Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301: 1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 55
    • 0342424729 scopus 로고    scopus 로고
    • A small protein that mediates the activation of a two-component system by another two-component system
    • Kox, L.F., Wosten, M.M., and Groisman, E.A. (2000) A small protein that mediates the activation of a two-component system by another two-component system. EMBO J 19: 1861-1872.
    • (2000) EMBO J , vol.19 , pp. 1861-1872
    • Kox, L.F.1    Wosten, M.M.2    Groisman, E.A.3
  • 56
    • 0016138377 scopus 로고
    • The barrier function of the gram-negative envelope
    • Leive, L. (1974) The barrier function of the gram-negative envelope. Ann NY Acad Sci 235: 109-129.
    • (1974) Ann NY Acad Sci , vol.235 , pp. 109-129
    • Leive, L.1
  • 57
    • 7644238048 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides: Anti-infective molecules of mammalian leukocytes
    • Levy, O. (2004) Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes. J Leukoc Biol 76: 909-925.
    • (2004) J Leukoc Biol , vol.76 , pp. 909-925
    • Levy, O.1
  • 59
  • 60
    • 0033870158 scopus 로고    scopus 로고
    • Overexpression of protease-deficient DegP (S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background
    • Misra, R., CastilloKeller, M., and Deng, M. (2000) Overexpression of protease-deficient DegP (S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J Bacterial 182: 4882-4888.
    • (2000) J Bacterial , vol.182 , pp. 4882-4888
    • Misra, R.1    Castillokeller, M.2    Deng, M.3
  • 61
    • 0036084367 scopus 로고    scopus 로고
    • MD-2, a novel accessory molecule, is involved in species-specific actions of Salmonella lipid A
    • Muroi, M., Ohnishi, T., and Tanamoto, K. (2002) MD-2, a novel accessory molecule, is involved in species-specific actions of Salmonella lipid A. Infect Immun 70: 3546-3550.
    • (2002) Infect Immun , vol.70 , pp. 3546-3550
    • Muroi, M.1    Ohnishi, T.2    Tanamoto, K.3
  • 62
    • 20244365945 scopus 로고    scopus 로고
    • Co-regulation of Salmonella enterica genes required for virulence and resistance to antimicrobial peptides by SIyA and PhoP/PhoQ
    • Navarre, W.W., Halsey, T.A., Walthers, D., Frye, J., McClelland, M., Potter, J.L., et al. (2005) Co-regulation of Salmonella enterica genes required for virulence and resistance to antimicrobial peptides by SIyA and PhoP/PhoQ. Mol Microbiol 56: 492-508.
    • (2005) Mol Microbiol , vol.56 , pp. 492-508
    • Navarre, W.W.1    Halsey, T.A.2    Walthers, D.3    Frye, J.4    McClelland, M.5    Potter, J.L.6
  • 63
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 64
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49: 1-32.
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 65
    • 0042355274 scopus 로고    scopus 로고
    • Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica
    • Parkhill, J., Sebaihia, M., Preston, A., Murphy, L.D., Thomson, N., Harris, D.E., et al. (2003) Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica. Nat Genet 35: 32-40.
    • (2003) Nat Genet , vol.35 , pp. 32-40
    • Parkhill, J.1    Sebaihia, M.2    Preston, A.3    Murphy, L.D.4    Thomson, N.5    Harris, D.E.6
  • 66
    • 0041929590 scopus 로고    scopus 로고
    • Structure and mechanism in prokaryotic mechanosensitive channels
    • Perozo, E., and Rees, D.C. (2003) Structure and mechanism in prokaryotic mechanosensitive channels. Curr Opin Struct Biol 13: 432-442.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 432-442
    • Perozo, E.1    Rees, D.C.2
  • 68
    • 2142646466 scopus 로고    scopus 로고
    • pagP is required for resistance to antibody-mediated complement lysis during Bordetella bronchiseptica respiratory infection
    • Pilione, M.R., Pishko, E.J., Preston, A., Maskell, D.J., and Harvill, E.T. (2004) pagP is required for resistance to antibody-mediated complement lysis during Bordetella bronchiseptica respiratory infection. Infect Immun 72: 2837-2842.
    • (2004) Infect Immun , vol.72 , pp. 2837-2842
    • Pilione, M.R.1    Pishko, E.J.2    Preston, A.3    Maskell, D.J.4    Harvill, E.T.5
  • 69
    • 0020481580 scopus 로고
    • Acyl and phosphoryl migration in lysophospholipids: Importance in phospholipid synthesis and phospholipase specificity
    • Pluckthun, A., and Dennis, E.A. (1982) Acyl and phosphoryl migration in lysophospholipids: importance in phospholipid synthesis and phospholipase specificity. Biochemistry 21: 1743-1750.
    • (1982) Biochemistry , vol.21 , pp. 1743-1750
    • Pluckthun, A.1    Dennis, E.A.2
  • 70
    • 0037673432 scopus 로고    scopus 로고
    • Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract
    • Preston, A., Maxim, E., Toland, E., Pishko, E.J., Harvill, E.T., Caroff, M., and Maskell, D.J. (2003) Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract. Mol Microbiol 48: 725-736.
    • (2003) Mol Microbiol , vol.48 , pp. 725-736
    • Preston, A.1    Maxim, E.2    Toland, E.3    Pishko, E.J.4    Harvill, E.T.5    Caroff, M.6    Maskell, D.J.7
  • 72
    • 0029087993 scopus 로고
    • Lipid A biosynthesis in Rhizobium leguminosarum: Role of a 2-keto-3-deoxyoctulosonate-activated 4′ phosphatase
    • Price, N.P., Jeyaretnam, B., Carlson, R.W., Kadrmas, J.L., Raetz, C.R., and Brozek, K.A. (1995) Lipid A biosynthesis in Rhizobium leguminosarum: role of a 2-keto-3-deoxyoctulosonate-activated 4′ phosphatase. Proc Natl Acad Sci USA 92: 7352-7356.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7352-7356
    • Price, N.P.1    Jeyaretnam, B.2    Carlson, R.W.3    Kadrmas, J.L.4    Raetz, C.R.5    Brozek, K.A.6
  • 73
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • Raetz, C.R., and Whitfield, C. (2002) Lipopolysaccharide endotoxins. Annu Rev Biochem 71: 635-700.
    • (2002) Annu Rev Biochem , vol.71 , pp. 635-700
    • Raetz, C.R.1    Whitfield, C.2
  • 74
    • 0026026516 scopus 로고
    • Membrane phospholipids as an energy source in the operation of the visual cycle
    • Rando, R.R. (1991) Membrane phospholipids as an energy source in the operation of the visual cycle. Biochemistry 30: 595-602.
    • (1991) Biochemistry , vol.30 , pp. 595-602
    • Rando, R.R.1
  • 76
    • 0034972212 scopus 로고    scopus 로고
    • Identification of Legionella pneumophila rep, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection
    • Robey, M., O'Connell, W., and Cianciotto, N.P. (2001) Identification of Legionella pneumophila rep, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection. Infect Immun 69: 4276-4286.
    • (2001) Infect Immun , vol.69 , pp. 4276-4286
    • Robey, M.1    O'Connell, W.2    Cianciotto, N.P.3
  • 77
    • 0018702835 scopus 로고
    • Interaction of divalent cations and polymyxin B with lipopolysaccharide
    • Schindler, M., and Osborn, M.J. (1979) Interaction of divalent cations and polymyxin B with lipopolysaccharide. Biochemistry 18: 4425-4430.
    • (1979) Biochemistry , vol.18 , pp. 4425-4430
    • Schindler, M.1    Osborn, M.J.2
  • 78
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz, G.E. (2002) The structure of bacterial outer membrane proteins. Biochim Biophys Acta 1565: 308-317.
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 79
    • 3142592449 scopus 로고    scopus 로고
    • PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B
    • Shi, Y., Cromie, M.J., Hsu, F.F., Turk, J., and Groisman, E.A. (2004) PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B. Mol Microbiol 53: 229-241.
    • (2004) Mol Microbiol , vol.53 , pp. 229-241
    • Shi, Y.1    Cromie, M.J.2    Hsu, F.F.3    Turk, J.4    Groisman, E.A.5
  • 80
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
    • Stover, C.K., Pham, X.Q., Erwin, A.L., Mizoguchi, S.D., Warrener, P., Mickey, M.J., et al. (2000) Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature 406: 959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1    Pham, X.Q.2    Erwin, A.L.3    Mizoguchi, S.D.4    Warrener, P.5    Mickey, M.J.6
  • 82
    • 0025976068 scopus 로고
    • Carboxyterminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyve, M., Moons, M., and Tommassen, J. (1991) Carboxyterminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218: 141-148.
    • (1991) J Mol Biol , vol.218 , pp. 141-148
    • Struyve, M.1    Moons, M.2    Tommassen, J.3
  • 83
    • 14844309359 scopus 로고    scopus 로고
    • Changes in lipopolysaccharide structure induce the sigma E-dependent response of Escherichia coli
    • Tarn, C., and Missiakas, D. (2005) Changes in lipopolysaccharide structure induce the sigma E-dependent response of Escherichia coli. Mol Microbiol 55: 1403-1412.
    • (2005) Mol Microbiol , vol.55 , pp. 1403-1412
    • Tarn, C.1    Missiakas, D.2
  • 84
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • Tamm, L.K., Hong, H., and Liang, B. (2004) Folding and assembly of beta-barrel membrane proteins. Biochim Biophys Acta 1666: 250-263.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 85
    • 0034653876 scopus 로고    scopus 로고
    • Salmonella-type heptaacylated lipid A is inactive and acts as an antagonist of lipopolysaccharide action on human line cells
    • Tanamoto, K., and Azumi, S. (2000) Salmonella-type heptaacylated lipid A is inactive and acts as an antagonist of lipopolysaccharide action on human line cells. J Immunol 164: 3149-3156.
    • (2000) J Immunol , vol.164 , pp. 3149-3156
    • Tanamoto, K.1    Azumi, S.2
  • 86
    • 14244253233 scopus 로고    scopus 로고
    • Lipopolysaccharide transport to the bacterial outer membrane in spheroplasts
    • Tefsen, B., Geurtsen, J., Beckers, F., Tommassen, J., and de Cock, H. (2005) Lipopolysaccharide transport to the bacterial outer membrane in spheroplasts. J Biol Chem 280: 4504-4509.
    • (2005) J Biol Chem , vol.280 , pp. 4504-4509
    • Tefsen, B.1    Geurtsen, J.2    Beckers, F.3    Tommassen, J.4    De Cock, H.5
  • 87
    • 2342542372 scopus 로고    scopus 로고
    • Biosynthesis, transport, and modification of lipid A
    • Trent, M.S. (2004) Biosynthesis, transport, and modification of lipid A. Biochem Cell Biol 82: 71-86.
    • (2004) Biochem Cell Biol , vol.82 , pp. 71-86
    • Trent, M.S.1
  • 88
    • 0035937824 scopus 로고    scopus 로고
    • A PhoP/PhoQ-induced lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium
    • Trent, M.S., Pabich, W., Raetz, C.R., and Miller, S.I. (2001) A PhoP/PhoQ-induced lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium. J Biol Chem 276: 9083-9092.
    • (2001) J Biol Chem , vol.276 , pp. 9083-9092
    • Trent, M.S.1    Pabich, W.2    Raetz, C.R.3    Miller, S.I.4
  • 89
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov, V., Hwang, P.M., and Kay, L.E. (2004) Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu Rev Biochem 73: 107-146.
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 91
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • Voulhoux, R., and Tommassen, J. (2004) Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly. Res Microbiol 155: 129-135.
    • (2004) Res Microbiol , vol.155 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 92
    • 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., Alba, B.M., Bose, B., Gross, C.A., and Sauer, R.T. (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
  • 93
    • 10344259135 scopus 로고    scopus 로고
    • MsbA transporter-dependent lipid A 1-dephosphorylation on the periplasmic surface of the inner membrane: Topography of Francisella novicida LpxE expressed in Escherichia coli
    • Wang, X., Karbarz, M.J., McGrath, S.C., Cotter, R.J., and Raetz, C.R. (2004) MsbA transporter-dependent lipid A 1-dephosphorylation on the periplasmic surface of the inner membrane: topography of Francisella novicida LpxE expressed in Escherichia coli. J Biol Chem 279: 49470-49478.
    • (2004) J Biol Chem , vol.279 , pp. 49470-49478
    • Wang, X.1    Karbarz, M.J.2    McGrath, S.C.3    Cotter, R.J.4    Raetz, C.R.5
  • 94
    • 10344224043 scopus 로고    scopus 로고
    • Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes
    • Winfield, M.D., and Groisman, E.A. (2004) Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes. Proc Natl Acad Sci USA 101: 17162-17167.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17162-17167
    • Winfield, M.D.1    Groisman, E.A.2
  • 95
    • 17644410810 scopus 로고    scopus 로고
    • Transcriptional regulation of the 4-amino-4-deoxy-L-arabinose biosynthetic genes in Yersinia pestis
    • Winfield, M.D., Latifi, T., and Groisman, E.A. (2005) Transcriptional regulation of the 4-amino-4-deoxy-L-arabinose biosynthetic genes in Yersinia pestis. J Biol Chem 280: 14765-14772.
    • (2005) J Biol Chem , vol.280 , pp. 14765-14772
    • Winfield, M.D.1    Latifi, T.2    Groisman, E.A.3
  • 96
    • 0034730333 scopus 로고    scopus 로고
    • A signal transduction system that responds to extracellular iron
    • Wosten, M.M., Kox, L.F., Chamnongpol, S., Soncini, F.C., and Groisman, E.A. (2000) A signal transduction system that responds to extracellular iron. Cell 103: 113-125.
    • (2000) Cell , vol.103 , pp. 113-125
    • Wosten, M.M.1    Kox, L.F.2    Chamnongpol, S.3    Soncini, F.C.4    Groisman, E.A.5
  • 97
    • 1342292545 scopus 로고    scopus 로고
    • The yersiniae - A model genus to study the rapid evolution of bacterial pathogens
    • Wren, B.W. (2003) The yersiniae - a model genus to study the rapid evolution of bacterial pathogens. Nat Rev Microbiol 1: 55-64.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 55-64
    • Wren, B.W.1
  • 98
    • 0032483819 scopus 로고    scopus 로고
    • Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases
    • Wyckoff, T.J., Lin, S., Cotter, R.J., Dotson, G.D., and Raetz, C.R. (1998) Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases. J Biol Chem 273: 32369-32372.
    • (1998) J Biol Chem , vol.273 , pp. 32369-32372
    • Wyckoff, T.J.1    Lin, S.2    Cotter, R.J.3    Dotson, G.D.4    Raetz, C.R.5
  • 99
    • 0037291906 scopus 로고    scopus 로고
    • Genes involved in the synthesis of the exopolysaccharide methanolan by the obligate methylotroph Methylobacillus sp strain 12S
    • Yoshida, T., Ayabe, Y., Yasunaga, M., Usami, Y., Habe, H., Nojiri, H., and Omori, T. (2003) Genes involved in the synthesis of the exopolysaccharide methanolan by the obligate methylotroph Methylobacillus sp strain 12S. Microbiology 149: 431-444.
    • (2003) Microbiology , vol.149 , pp. 431-444
    • Yoshida, T.1    Ayabe, Y.2    Yasunaga, M.3    Usami, Y.4    Habe, H.5    Nojiri, H.6    Omori, T.7
  • 100
    • 0029451046 scopus 로고
    • The lipopolysaccharide of Legionella pneumophila serogroup 1 (strain Philadelphia 1): Chemical structure and biological significance
    • Zahringer, U., Knirel, Y.A., Lindner, B., Heibig, J.H., Sonesson, A., Marre, R., and Rietschel, E.T. (1995) The lipopolysaccharide of Legionella pneumophila serogroup 1 (strain Philadelphia 1): chemical structure and biological significance. Prog Clin Biol Res 392: 113-139.
    • (1995) Prog Clin Biol Res , vol.392 , pp. 113-139
    • Zahringer, U.1    Knirel, Y.A.2    Lindner, B.3    Heibig, J.H.4    Sonesson, A.5    Marre, R.6    Rietschel, E.T.7
  • 101
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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