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Volumn 197, Issue 10, 2015, Pages 1705-1715

Revisiting the gram-negative lipoprotein paradigm

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; GLOBOMYCIN; LIPOPROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN LOLC; PROTEIN LOLE; PROTEIN TUL4A; PROTEIN TUL4B; RIFAMPICIN; UNCLASSIFIED DRUG; ACYLTRANSFERASE; APOLIPOPROTEIN N-ACYLTRANSFERASE; CULTURE MEDIUM;

EID: 84928528034     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02414-14     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 33745847180 scopus 로고    scopus 로고
    • TLRs, NLRs and RLRs: a trinity of pathogen sensors that co-operate in innate immunity
    • Creagh EM, O'Neill LA. 2006. TLRs, NLRs and RLRs: a trinity of pathogen sensors that co-operate in innate immunity. Trends Immunol 27:352-357. http://dx.doi.org/10.1016/j.it.2006.06.003.
    • (2006) Trends Immunol , vol.27 , pp. 352-357
    • Creagh, E.M.1    O'Neill, L.A.2
  • 3
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-B by Toll-like receptors
    • Kawai T, Akira S. 2007. Signaling to NF-B by Toll-like receptors. Trends Mol Med 13:460-469. http://dx.doi.org/10.1016/j.molmed.2007.09.002.
    • (2007) Trends Mol Med , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 4
    • 84902276774 scopus 로고    scopus 로고
    • Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond
    • Zuckert WR. 2014. Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond. Biochim Biophys Acta 1843:1509-1516. http://dx.doi.org/10.1016/j.bbamcr.2014.04.022.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1509-1516
    • Zuckert, W.R.1
  • 5
    • 31844431988 scopus 로고    scopus 로고
    • An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals
    • Narita S, Tokuda H. 2006. An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals. FEBS Lett 580:1164-1170. http://dx.doi.org/10.1016/j.febslet.2005.10.038.
    • (2006) FEBS Lett , vol.580 , pp. 1164-1170
    • Narita, S.1    Tokuda, H.2
  • 6
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H. 2000. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2:212-218. http://dx.doi.org/10.1038/35008635.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 7
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda S, Tokuda H. 2009. Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc Natl Acad SciUSA 106:5877-5882. http://dx.doi.org/10.1073/pnas.0900896106.
    • (2009) Proc Natl Acad SciUSA , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 8
    • 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, Yokota N, Matsuyama S, Tokuda H. 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. http://dx.doi.org/10.1016/S0014-5793(98)01334-9.
    • (1998) FEBS Lett , vol.439 , pp. 51-54
    • Tajima, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 9
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita S, Tokuda H. 2007. Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem 282:13372-13378. http://dx.doi.org/10.1074/jbc. M611839200.
    • (2007) J Biol Chem , vol.282 , pp. 13372-13378
    • Narita, S.1    Tokuda, H.2
  • 10
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • Seydel A, Gounon P, Pugsley AP. 1999. Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection. Mol Microbiol 34:810-821. http://dx.doi.org/10.1046/j.1365-2958.1999.01647.x.
    • (1999) Mol Microbiol , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 11
    • 42949086603 scopus 로고    scopus 로고
    • Identification of Francisella tularensis lipoproteins that stimulate the tolllike receptor (TLR) 2/TLR1 heterodimer
    • Thakran S, Li H, Lavine CL, Miller MA, Bina JE, Bina XR, Re F. 2008. Identification of Francisella tularensis lipoproteins that stimulate the tolllike receptor (TLR) 2/TLR1 heterodimer. J Biol Chem 283:3751-3760. http://dx.doi.org/10.1074/jbc. M706854200.
    • (2008) J Biol Chem , vol.283 , pp. 3751-3760
    • Thakran, S.1    Li, H.2    Lavine, C.L.3    Miller, M.A.4    Bina, J.E.5    Bina, X.R.6    Re, F.7
  • 12
    • 79951809756 scopus 로고    scopus 로고
    • The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli
    • Cowles CE, Li Y, Semmelhack MF, Cristea IM, Silhavy TJ. 2011. The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli. Mol Microbiol 79:1168-1181. http://dx.doi.org/10.1111/j.1365-2958.2011.07539.x.
    • (2011) Mol Microbiol , vol.79 , pp. 1168-1181
    • Cowles, C.E.1    Li, Y.2    Semmelhack, M.F.3    Cristea, I.M.4    Silhavy, T.J.5
  • 14
    • 2642553745 scopus 로고    scopus 로고
    • Outer membrane proteins of pathogenic spirochetes
    • Cullen PA, Haake DA, Adler B. 2004. Outer membrane proteins of pathogenic spirochetes. FEMS Microbiol Rev 28:291-318. http://dx.doi.org/10.1016/j.femsre.2003.10.004.
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 291-318
    • Cullen, P.A.1    Haake, D.A.2    Adler, B.3
  • 15
    • 79951905038 scopus 로고    scopus 로고
    • Structural evidence of alpha-aminoacylated lipoproteins of Staphylococcus aureus
    • Asanuma M, Kurokawa K, Ichikawa R, Ryu KH, Chae JH, Dohmae N, Lee BL, Nakayama H. 2011. Structural evidence of alpha-aminoacylated lipoproteins of Staphylococcus aureus. FEBS J 278:716-728. http://dx.doi.org/10.1111/j.1742-4658.2010.07990.x.
    • (2011) FEBS J , vol.278 , pp. 716-728
    • Asanuma, M.1    Kurokawa, K.2    Ichikawa, R.3    Ryu, K.H.4    Chae, J.H.5    Dohmae, N.6    Lee, B.L.7    Nakayama, H.8
  • 16
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em
    • Hutchings MI, Palmer T, Harrington DJ, Sutcliffe IC. 2009. Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em. Trends Microbiol 17:13-21. http://dx.doi.org/10.1016/j.tim.2008.10.001.
    • (2009) Trends Microbiol , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 17
    • 84864009033 scopus 로고    scopus 로고
    • Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus
    • Kurokawa K, Kim MS, Ichikawa R, Ryu KH, Dohmae N, Nakayama H, Lee BL. 2012. Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus. J Bacteriol 194:3299-3306. http://dx.doi.org/10.1128/JB.00314-12.
    • (2012) J Bacteriol , vol.194 , pp. 3299-3306
    • Kurokawa, K.1    Kim, M.S.2    Ichikawa, R.3    Ryu, K.H.4    Dohmae, N.5    Nakayama, H.6    Lee, B.L.7
  • 18
    • 33947413501 scopus 로고    scopus 로고
    • Lipoprotein synthesis in mycobacteria
    • Rezwan M, Grau T, Tschumi A, Sander P. 2007. Lipoprotein synthesis in mycobacteria. Microbiology 153:652-658. http://dx.doi.org/10.1099/mic.0.2006/000216-0.
    • (2007) Microbiology , vol.153 , pp. 652-658
    • Rezwan, M.1    Grau, T.2    Tschumi, A.3    Sander, P.4
  • 20
    • 33750934728 scopus 로고    scopus 로고
    • Genetic tools for highly pathogenic Francisella tularensis subsp
    • LoVullo ED, Sherrill LA, Perez LL, Pavelka MS, Jr. 2006. Genetic tools for highly pathogenic Francisella tularensis subsp. tularensis. Microbiology 152:3425-3435. http://dx.doi.org/10.1099/mic.0.29121-0.
    • (2006) tularensis. Microbiology , vol.152 , pp. 3425-3435
    • LoVullo, E.D.1    Sherrill, L.A.2    Perez, L.L.3    Pavelka, M.S.4
  • 21
    • 38849127470 scopus 로고    scopus 로고
    • cis- and trans-acting elements involved in regulation of norB (norZ), the gene encoding nitric oxide reductase in Neisseria gonorrhoeae
    • Isabella V, Wright LF, Barth K, Spence JM, Grogan S, Genco CA, Clark VL. 2008. cis- and trans-acting elements involved in regulation of norB (norZ), the gene encoding nitric oxide reductase in Neisseria gonorrhoeae. Microbiology 154:226-239. http://dx.doi.org/10.1099/mic.0.2007/010470-0.
    • (2008) Microbiology , vol.154 , pp. 226-239
    • Isabella, V.1    Wright, L.F.2    Barth, K.3    Spence, J.M.4    Grogan, S.5    Genco, C.A.6    Clark, V.L.7
  • 22
    • 33846231766 scopus 로고    scopus 로고
    • Characterization of Francisella tularensis outer membrane proteins
    • Huntley JF, Conley PG, Hagman KE, Norgard MV. 2007. Characterization of Francisella tularensis outer membrane proteins. J Bacteriol 189:561-574. http://dx.doi.org/10.1128/JB.01505-06.
    • (2007) J Bacteriol , vol.189 , pp. 561-574
    • Huntley, J.F.1    Conley, P.G.2    Hagman, K.E.3    Norgard, M.V.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. http://dx.doi.org/10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 33846504443 scopus 로고    scopus 로고
    • A comprehensive transposon mutant library of Francisella novicida, a bioweapon surrogate
    • Gallagher LA, Ramage E, Jacobs MA, Kaul R, Brittnacher M, Manoil C. 2007. A comprehensive transposon mutant library of Francisella novicida, a bioweapon surrogate. Proc Natl Acad Sci U S A 104:1009-1014. http://dx.doi.org/10.1073/pnas.0606713104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1009-1014
    • Gallagher, L.A.1    Ramage, E.2    Jacobs, M.A.3    Kaul, R.4    Brittnacher, M.5    Manoil, C.6
  • 25
    • 0026920427 scopus 로고
    • The 17 kDa lipoprotein and encoding gene of Francisella tularensis LVS are conserved in strains of Francisella tularensis
    • Sjostedt A, Kuoppa K, Johansson T, Sandstrom G. 1992. The 17 kDa lipoprotein and encoding gene of Francisella tularensis LVS are conserved in strains of Francisella tularensis. Microb Pathog 13:243-249. http://dx.doi.org/10.1016/0882-4010(92)90025-J.
    • (1992) Microb Pathog , vol.13 , pp. 243-249
    • Sjostedt, A.1    Kuoppa, K.2    Johansson, T.3    Sandstrom, G.4
  • 26
    • 0025784566 scopus 로고
    • The T-cell-stimulating 17-kilodalton protein of Francisella tularensis LVS is a lipoprotein
    • Sjostedt A, Tarnvik A, Sandstrom G. 1991. The T-cell-stimulating 17-kilodalton protein of Francisella tularensis LVS is a lipoprotein. Infect Immun 59:3163-3168.
    • (1991) Infect Immun , vol.59 , pp. 3163-3168
    • Sjostedt, A.1    Tarnvik, A.2    Sandstrom, G.3
  • 27
    • 0017836107 scopus 로고
    • Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein
    • Yem DW, Wu HC. 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
  • 29
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cascales E, Bernadac A, Gavioli M, Lazzaroni JC, Lloubes R. 2002. Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J Bacteriol 184:754-759. http://dx.doi.org/10.1128/JB.184.3.754-759.2002.
    • (2002) J Bacteriol , vol.184 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.C.4    Lloubes, R.5
  • 30
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide
    • Charlson ES, Werner JN, Misra R. 2006. Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide. J Bacteriol 188:7186-7194. http://dx.doi.org/10.1128/JB.00571-06.
    • (2006) J Bacteriol , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 31
    • 68249111866 scopus 로고    scopus 로고
    • Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria:function, structure, role in pathogenesis and potential application in immunoprophylaxis
    • Godlewska R, Wisniewska K, Pietras Z, Jagusztyn-Krynicka EK. 2009. Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria:function, structure, role in pathogenesis and potential application in immunoprophylaxis. FEMS Microbiol Lett 298:1-11. http://dx.doi.org/10.1111/j.1574-6968.2009.01659.x.
    • (2009) FEMS Microbiol Lett , vol.298 , pp. 1-11
    • Godlewska, R.1    Wisniewska, K.2    Pietras, Z.3    Jagusztyn-Krynicka, E.K.4
  • 32
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A 103:11754-11759. http://dx.doi.org/10.1073/pnas.0604744103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6
  • 34
    • 0030968582 scopus 로고    scopus 로고
    • Subunit II of the cytochrome bo3 ubiquinol oxidase from Escherichia coli is a lipoprotein
    • Ma J, Katsonouri A, Gennis RB. 1997. Subunit II of the cytochrome bo3 ubiquinol oxidase from Escherichia coli is a lipoprotein. Biochemistry 36:11298-11303. http://dx.doi.org/10.1021/bi9709710.
    • (1997) Biochemistry , vol.36 , pp. 11298-11303
    • Ma, J.1    Katsonouri, A.2    Gennis, R.B.3
  • 35
    • 58149299623 scopus 로고    scopus 로고
    • Improved shuttle vectors for Francisella tularensis genetics
    • LoVullo ED, Sherrill LA, Pavelka MS, Jr. 2009. Improved shuttle vectors for Francisella tularensis genetics. FEMS Microbiol Lett 291:95-102. http://dx.doi.org/10.1111/j.1574-6968.2008.01440.x.
    • (2009) FEMS Microbiol Lett , vol.291 , pp. 95-102
    • LoVullo, E.D.1    Sherrill, L.A.2    Pavelka, M.S.3
  • 36
    • 0031596298 scopus 로고    scopus 로고
    • MglA and MglB are required for the intramacrophage growth of Francisella novicida
    • Baron GS, Nano FE. 1998. MglA and MglB are required for the intramacrophage growth of Francisella novicida. Mol Microbiol 29:247-259. http://dx.doi.org/10.1046/j.1365-2958.1998.00926.x.
    • (1998) Mol Microbiol , vol.29 , pp. 247-259
    • Baron, G.S.1    Nano, F.E.2
  • 38
    • 34748903561 scopus 로고    scopus 로고
    • Innate and adaptive immunity to Francisella
    • Elkins KL, Cowley SC, Bosio CM. 2007. Innate and adaptive immunity to Francisella. Ann N Y Acad Sci 1105:284-324. http://dx.doi.org/10.1196/annals.1409.014.
    • (2007) Ann N Y Acad Sci , vol.1105 , pp. 284-324
    • Elkins, K.L.1    Cowley, S.C.2    Bosio, C.M.3
  • 39
    • 33646357470 scopus 로고    scopus 로고
    • Toll-like receptor 2 is required for inflammatory responses to Francisella tularensis LVS
    • Katz J, Zhang P, Martin M, Vogel SN, Michalek SM. 2006. Toll-like receptor 2 is required for inflammatory responses to Francisella tularensis LVS. Infect Immun 74:2809-2816. http://dx.doi.org/10.1128/IAI.74.5.2809-2816.2006.
    • (2006) Infect Immun , vol.74 , pp. 2809-2816
    • Katz, J.1    Zhang, P.2    Martin, M.3    Vogel, S.N.4    Michalek, S.M.5
  • 40
    • 0029976378 scopus 로고    scopus 로고
    • An essential role for actA in acid tolerance of Rhizobium meliloti
    • Tiwari RP, Reeve WG, Dilworth MJ, Glenn AR. 1996. An essential role for actA in acid tolerance of Rhizobium meliloti. Microbiology 142:601-610. http://dx.doi.org/10.1099/13500872-142-3-601.
    • (1996) Microbiology , vol.142 , pp. 601-610
    • Tiwari, R.P.1    Reeve, W.G.2    Dilworth, M.J.3    Glenn, A.R.4
  • 41
    • 69249119399 scopus 로고    scopus 로고
    • Wolbachia lipoprotein stimulates innate and adaptive immunity through Toll-like receptors 2 and 6 to induce disease manifestations of filariasis
    • Turner JD, Langley RS, Johnston KL, Gentil K, Ford L, Wu B, Graham M, Sharpley F, Slatko B, Pearlman E, Taylor MJ. 2009. Wolbachia lipoprotein stimulates innate and adaptive immunity through Toll-like receptors 2 and 6 to induce disease manifestations of filariasis. J Biol Chem 284:22364-22378. http://dx.doi.org/10.1074/jbc. M901528200.
    • (2009) J Biol Chem , vol.284 , pp. 22364-22378
    • Turner, J.D.1    Langley, R.S.2    Johnston, K.L.3    Gentil, K.4    Ford, L.5    Wu, B.6    Graham, M.7    Sharpley, F.8    Slatko, B.9    Pearlman, E.10    Taylor, M.J.11
  • 42
    • 70350446622 scopus 로고    scopus 로고
    • Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE
    • Yasuda M, Iguchi-Yokoyama A, Matsuyama S, Tokuda H, Narita S. 2009. Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE. Biosci Biotechnol Biochem 73:2310-2316. http://dx.doi.org/10.1271/bbb.90451.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 2310-2316
    • Yasuda, M.1    Iguchi-Yokoyama, A.2    Matsuyama, S.3    Tokuda, H.4    Narita, S.5
  • 44
    • 0026482027 scopus 로고
    • The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein
    • Hoehn GT, Clark VL. 1992. The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein. Infect Immun 60:4704-4708.
    • (1992) Infect Immun , vol.60 , pp. 4704-4708
    • Hoehn, G.T.1    Clark, V.L.2
  • 45
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon C, Vidal-Ingigliardi D, Pugsley AP. 2005. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J Biol Chem 280:974-983. http://dx.doi.org/10.1074/jbc. M411059200.
    • (2005) J Biol Chem , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 46
    • 0027296627 scopus 로고
    • Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification
    • Gan K, Gupta SD, Sankaran K, Schmid MB, Wu HC. 1993. Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification. J Biol Chem 268:16544-16550.
    • (1993) J Biol Chem , vol.268 , pp. 16544-16550
    • Gan, K.1    Gupta, S.D.2    Sankaran, K.3    Schmid, M.B.4    Wu, H.C.5
  • 47
    • 0019378291 scopus 로고
    • Globomycin sensitivity of Escherichia coli and Salmonella typhimurium:effects of mutations affecting structures of murein lipoprotein
    • Lai JS, Philbrick WM, Hayashi S, Inukai M, Arai M, Hirota Y, Wu HC. 1981. Globomycin sensitivity of Escherichia coli and Salmonella typhimurium:effects of mutations affecting structures of murein lipoprotein. J Bacteriol 145:657-660.
    • (1981) J Bacteriol , vol.145 , pp. 657-660
    • Lai, J.S.1    Philbrick, W.M.2    Hayashi, S.3    Inukai, M.4    Arai, M.5    Hirota, Y.6    Wu, H.C.7
  • 48
    • 84871722765 scopus 로고    scopus 로고
    • Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex
    • Mizutani M, Mukaiyama K, Xiao J, Mori M, Satou R, Narita S, Okuda S, Tokuda H. 2013. Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex. FEBS Lett 587:23-29. http://dx.doi.org/10.1016/j.febslet.2012.11.009.
    • (2013) FEBS Lett , vol.587 , pp. 23-29
    • Mizutani, M.1    Mukaiyama, K.2    Xiao, J.3    Mori, M.4    Satou, R.5    Narita, S.6    Okuda, S.7    Tokuda, H.8
  • 49
    • 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, Tanaka K, Matsuyama S, Tokuda H. 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. http://dx.doi.org/10.1128/JB.184.5.1417-1422.2002.
    • (2002) J Bacteriol , vol.184 , pp. 1417-1422
    • Narita, S.1    Tanaka, K.2    Matsuyama, S.3    Tokuda, H.4
  • 50
    • 0019309069 scopus 로고
    • Accumulation of glyceridecontaining 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 glyceridecontaining 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
  • 52
    • 33751532631 scopus 로고    scopus 로고
    • Innate immune response to Francisella tularensis is mediated by TLR2 and caspase-1 activation
    • Li H, Nookala S, Bina XR, Bina JE, Re F. 2006. Innate immune response to Francisella tularensis is mediated by TLR2 and caspase-1 activation. J Leukoc Biol 80:766-773. http://dx.doi.org/10.1189/jlb.0406294.
    • (2006) J Leukoc Biol , vol.80 , pp. 766-773
    • Li, H.1    Nookala, S.2    Bina, X.R.3    Bina, J.E.4    Re, F.5
  • 53
    • 33646472970 scopus 로고    scopus 로고
    • Myeloid differentiation factor-88 (MyD88) is essential for control of primary in vivo Francisella tularensis LVS infection, but not for control of intra-macrophage bacterial replication
    • Collazo CM, Sher A, Meierovics AI, Elkins KL. 2006. Myeloid differentiation factor-88 (MyD88) is essential for control of primary in vivo Francisella tularensis LVS infection, but not for control of intra-macrophage bacterial replication. Microbes Infect 8:779-790. http://dx.doi.org/10.1016/j.micinf.2005.09.014.
    • (2006) Microbes Infect , vol.8 , pp. 779-790
    • Collazo, C.M.1    Sher, A.2    Meierovics, A.I.3    Elkins, K.L.4
  • 54
    • 33646911624 scopus 로고    scopus 로고
    • Toll-like receptor 2 is required for control of pulmonary infection with Francisella tularensis
    • Malik M, Bakshi CS, Sahay B, Shah A, Lotz SA, Sellati TJ. 2006. Toll-like receptor 2 is required for control of pulmonary infection with Francisella tularensis. Infect Immun 74:3657-3662. http://dx.doi.org/10.1128/IAI.02030-05.
    • (2006) Infect Immun , vol.74 , pp. 3657-3662
    • Malik, M.1    Bakshi, C.S.2    Sahay, B.3    Shah, A.4    Lotz, S.A.5    Sellati, T.J.6
  • 55
    • 34547636340 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated signaling requirements for Francisella tularensis live vaccine strain infec- tion of murine macrophages
    • Cole LE, Shirey KA, Barry E, Santiago A, Rallabhandi P, Elkins KL, Puche AC, Michalek SM, Vogel SN. 2007. Toll-like receptor 2-mediated signaling requirements for Francisella tularensis live vaccine strain infec- tion of murine macrophages. Infect Immun 75:4127-4137. http://dx.doi.org/10.1128/IAI.01868-06.
    • (2007) Infect Immun , vol.75 , pp. 4127-4137
    • Cole, L.E.1    Shirey, K.A.2    Barry, E.3    Santiago, A.4    Rallabhandi, P.5    Elkins, K.L.6    Puche, A.C.7    Michalek, S.M.8    Vogel, S.N.9
  • 56
    • 1542782546 scopus 로고    scopus 로고
    • Maturation of lipoproteins by type II signal peptidase is required for phagosomal escape of Listeria monocytogenes
    • Reglier-Poupet H, Frehel C, Dubail I, Beretti JL, Berche P, Charbit A, Raynaud C. 2003. Maturation of lipoproteins by type II signal peptidase is required for phagosomal escape of Listeria monocytogenes. J Biol Chem 278:49469-49477. http://dx.doi.org/10.1074/jbc. M307953200.
    • (2003) J Biol Chem , vol.278 , pp. 49469-49477
    • Reglier-Poupet, H.1    Frehel, C.2    Dubail, I.3    Beretti, J.L.4    Berche, P.5    Charbit, A.6    Raynaud, C.7
  • 58
    • 65649147179 scopus 로고    scopus 로고
    • Single-copy chromosomal integration systems for Francisella tularensis
    • LoVullo ED, Molins-Schneekloth CR, Schweizer HP, Pavelka MS, Jr. 2009. Single-copy chromosomal integration systems for Francisella tularensis. Microbiology 155:1152-1163. http://dx.doi.org/10.1099/mic.0.022491-0.
    • (2009) Microbiology , vol.155 , pp. 1152-1163
    • LoVullo, E.D.1    Molins-Schneekloth, C.R.2    Schweizer, H.P.3    Pavelka, M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.