메뉴 건너뛰기




Volumn 61, Issue , 2007, Pages 191-214

Biogenesis of the gram-negative bacterial outer membrane

Author keywords

Lipopolysaccharide; Lipoproteins; Outer membrane proteins; Phospholipids

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; LIPOPROTEIN; MEMBRANE PHOSPHOLIPID; OUTER MEMBRANE PROTEIN;

EID: 35348906348     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.61.080706.093245     Document Type: Review
Times cited : (378)

References (116)
  • 1
    • 0037516675 scopus 로고    scopus 로고
    • n-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane
    • Abe S, Okutsu T, Nakajima H, Kakuda N, Ohtsu I, et al. 2003. n-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane. Microbiology 149:1265-73
    • (2003) Microbiology , vol.149 , pp. 1265-1273
    • Abe, S.1    Okutsu, T.2    Nakajima, H.3    Kakuda, N.4    Ohtsu, I.5
  • 2
    • 0015973774 scopus 로고
    • Protein composition of the outer membrane of Salmonella typhimurium: Effect of lipopolysaccharide mutations
    • Ames GFL, Spudich EN, Nikaido H. 1974. Protein composition of the outer membrane of Salmonella typhimurium: effect of lipopolysaccharide mutations. J. Bacteriol. 117:406-16
    • (1974) J. Bacteriol , vol.117 , pp. 406-416
    • Ames, G.F.L.1    Spudich, E.N.2    Nikaido, H.3
  • 4
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • Bayer ME. 1968. Areas of adhesion between wall and membrane of Escherichia coli. J. Gen. Microbiol. 53:395-404
    • (1968) J. Gen. Microbiol , vol.53 , pp. 395-404
    • Bayer, M.E.1
  • 5
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens S, Maier R, de Cock H, Schmid FX, Gross CA. 2001. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20:285-94
    • (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
  • 6
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel E, Doeven MK, Poolman B. 2006. ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett. 580:1023-35
    • (2006) FEBS Lett , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 7
    • 0037615052 scopus 로고    scopus 로고
    • Secretins of Pseudomonas aeruginosa: Large holes in the outer membrane
    • Bitter W. 2003. Secretins of Pseudomonas aeruginosa: large holes in the outer membrane. Arch. Microbiol. 179:307-14
    • (2003) Arch. Microbiol , vol.179 , pp. 307-314
    • Bitter, W.1
  • 8
    • 0024119777 scopus 로고
    • The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis
    • Bolla JM, Lazdunski C, Pagès JM. 1988. The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis. EMBO J. 7:3595-99
    • (1988) EMBO J , vol.7 , pp. 3595-3599
    • Bolla, J.M.1    Lazdunski, C.2    Pagès, J.M.3
  • 9
    • 3042554408 scopus 로고    scopus 로고
    • Identification of an outer membrane protein required for lipopolysaccharide transport to the bacterial cell surface
    • Bos MP, Tefsen B, Geurtsen J, Tommassen J. 2004. Identification of an outer membrane protein required for lipopolysaccharide transport to the bacterial cell surface. Proc. Natl. Acad. Sci. USA 101:9417-22
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9417-9422
    • Bos, M.P.1    Tefsen, B.2    Geurtsen, J.3    Tommassen, J.4
  • 10
    • 35848941316 scopus 로고    scopus 로고
    • Bos MP, Tommassen J. 2006. Identification of LPS transport components in Neisseria meningitidis. In Fifteenth Int. Pathogenic Neisseria Conf., ed. J Davies, M Jennings, pp. 33. West Leederville, Australia: Cambridge Publ.
    • Bos MP, Tommassen J. 2006. Identification of LPS transport components in Neisseria meningitidis. In Fifteenth Int. Pathogenic Neisseria Conf., ed. J Davies, M Jennings, pp. 33. West Leederville, Australia: Cambridge Publ.
  • 11
    • 0036046150 scopus 로고    scopus 로고
    • Imp/OstA is required for cell envelope biogenesis in Escherichia coli
    • Braun M, Silhavy TJ. 2002. Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol. Microbiol. 45:1289-302
    • (2002) Mol. Microbiol , vol.45 , pp. 1289-1302
    • Braun, M.1    Silhavy, T.J.2
  • 12
    • 0033757708 scopus 로고    scopus 로고
    • Borrelia genomes in the year 2000
    • Casjens S. 2000. Borrelia genomes in the year 2000. J. Mol. Microbiol. Biotechnol. 2:401-10
    • (2000) J. Mol. Microbiol. Biotechnol , vol.2 , pp. 401-410
    • Casjens, S.1
  • 13
    • 0037214416 scopus 로고    scopus 로고
    • Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture
    • CastilloKeller M, Misra R. 2003. Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture. J. Bacteriol. 185:148-54
    • (2003) J. Bacteriol , vol.185 , pp. 148-154
    • CastilloKeller, M.1    Misra, R.2
  • 14
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami M, Guilvout I, Gregorini M, Remigy HW, Müller SA, et al. 2005. Structural insights into the secretin PulD and its trypsin-resistant core. J. Biol. Chem. 280:37732-41
    • (2005) J. Biol. Chem , vol.280 , pp. 37732-37741
    • Chami, M.1    Guilvout, I.2    Gregorini, M.3    Remigy, H.W.4    Müller, S.A.5
  • 15
    • 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. 188:7186-94
    • (2006) J. Bacteriol , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 16
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli binds a class of outer membrane proteins
    • Chen R, Henning U. 1996. A periplasmic protein (Skp) of Escherichia coli binds a class of outer membrane proteins. Mal. Microbiol. 19:1287-94
    • (1996) Mal. Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 17
    • 0037797311 scopus 로고    scopus 로고
    • Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: Identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide
    • Cox AD, Wright JC, Li J, Hood DW, Moxon ER, Richards JC. 2003. Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide. J. Bacteriol. 185:3270-77
    • (2003) J. Bacteriol , vol.185 , pp. 3270-3277
    • Cox, A.D.1    Wright, J.C.2    Li, J.3    Hood, D.W.4    Moxon, E.R.5    Richards, J.C.6
  • 18
    • 0242693130 scopus 로고    scopus 로고
    • Bacterial membrane lipids: Where do we stand?
    • Cronan JE. 2003. Bacterial membrane lipids: Where do we stand? Annu. Rev. Microbiol. 57:203-24
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 203-224
    • Cronan, J.E.1
  • 19
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue C, Raina S. 1998. A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 17:3968-80
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 20
    • 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, Schäfer U, Potgeter M, Demel R, Müller M, et al. 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    Schäfer, U.2    Potgeter, M.3    Demel, R.4    Müller, M.5
  • 21
    • 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, Struyvé M, Kleerebezem M, van der Krift T, 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. 269:473-78
    • (1997) J. Mol. Biol , vol.269 , pp. 473-478
    • De Cock, H.1    Struyvé, M.2    Kleerebezem, M.3    van der Krift, T.4    Tommassen, J.5
  • 22
    • 0029903977 scopus 로고    scopus 로고
    • Lipopolysaccharides and divalent cations are involved in the formation of an assembly-competent intermediate of outer membrane protein PhoE of E. coli
    • De Cock H, Tommassen J. 1996. Lipopolysaccharides and divalent cations are involved in the formation of an assembly-competent intermediate of outer membrane protein PhoE of E. coli. EMBO J. 15:5567-73
    • (1996) EMBO J , vol.15 , pp. 5567-5573
    • De Cock, H.1    Tommassen, J.2
  • 24
    • 0021209199 scopus 로고
    • Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli
    • Dev IK, Ray PH. 1984. Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B. J. Biol. Chem. 259: 11114-20
    • (1984) B. J. Biol. Chem , vol.259 , pp. 11114-11120
    • Dev, I.K.1    Ray, P.H.2
  • 25
    • 33645836299 scopus 로고    scopus 로고
    • Lipid trafficking to the outer membrane of gram-negative bacteria
    • Doerrler WT. 2006. Lipid trafficking to the outer membrane of gram-negative bacteria. Mol. Microbiol. 60:542-52
    • (2006) Mol. Microbiol , vol.60 , pp. 542-552
    • Doerrler, W.T.1
  • 26
    • 7244248683 scopus 로고    scopus 로고
    • MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli
    • Doerrler WT, Gibbons HS, Raetz CRH. 2004. MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli. J. Biol. Chem. 276:45102-9
    • (2004) J. Biol. Chem , vol.276 , pp. 45102-45109
    • Doerrler, W.T.1    Gibbons, H.S.2    Raetz, C.R.H.3
  • 27
    • 23044501295 scopus 로고    scopus 로고
    • Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant
    • Doerrler WT, Raetz CRH. 2005. Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J. Biol. Chem. 280:27679-87
    • (2005) J. Biol. Chem , vol.280 , pp. 27679-27687
    • Doerrler, W.T.1    Raetz, C.R.H.2
  • 28
    • 33750892424 scopus 로고    scopus 로고
    • Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein
    • Dong C, Beis K, Nesper J, Brunkan-Lamontagne AL, Clarke BR, et al. 2006. Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein. Nature 444:226-29
    • (2006) Nature , vol.444 , pp. 226-229
    • Dong, C.1    Beis, K.2    Nesper, J.3    Brunkan-Lamontagne, A.L.4    Clarke, B.R.5
  • 29
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • Eggert US, Ruiz N, Falcone BV, Branstrom AA, Goldman RC, et al. 2001. Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin. Science 294:361-64
    • (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
  • 30
    • 0030756034 scopus 로고    scopus 로고
    • Folding of a bacterial outer membrane protein during passage through the periplasm
    • Eppens EF, Nouwen N, Tommassen J. 1997. Folding of a bacterial outer membrane protein during passage through the periplasm. EMBO J. 16:4295-301
    • (1997) EMBO J , vol.16 , pp. 4295-4301
    • Eppens, E.F.1    Nouwen, N.2    Tommassen, J.3
  • 32
    • 0029867376 scopus 로고    scopus 로고
    • A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae
    • Fussenegger M, Facius D, Meier J, Meyer TF. 1996. A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae. Mol. Microbiol. 19:1095-105
    • (1996) Mol. Microbiol , vol.19 , pp. 1095-1105
    • Fussenegger, M.1    Facius, D.2    Meier, J.3    Meyer, T.F.4
  • 33
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I, Gabriel K, Beech P, Waller R, Lithgow T. 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
  • 34
    • 0018365893 scopus 로고
    • A lipopolysaccharide- binding cell-surface protein from Salmonella minnesota. Isolation, partial characterization and occurrence in different Enterobacteriaceae
    • Geyer R, Galanos C, Westphal O, Golecki JR. 1979. A lipopolysaccharide- binding cell-surface protein from Salmonella minnesota. Isolation, partial characterization and occurrence in different Enterobacteriaceae. Eur. J. Biochem. 98:27-38
    • (1979) Eur. J. Biochem , vol.98 , pp. 27-38
    • Geyer, R.1    Galanos, C.2    Westphal, O.3    Golecki, J.R.4
  • 35
    • 33646593149 scopus 로고    scopus 로고
    • Ecf, an alternative sigma factor from Neisseria gonorrhoeae, controls expression of msrAB, which encodes methionine sulfoxide reductase
    • Gunesekere IC, Kahler CM, Ryan CS, Snyder LA, Saunders NJ, et al. 2006. Ecf, an alternative sigma factor from Neisseria gonorrhoeae, controls expression of msrAB, which encodes methionine sulfoxide reductase. J. Bacteriol. 188:3463-69
    • (2006) J. Bacteriol , vol.188 , pp. 3463-3469
    • Gunesekere, I.C.1    Kahler, C.M.2    Ryan, C.S.3    Snyder, L.A.4    Saunders, N.J.5
  • 36
    • 0027185234 scopus 로고
    • Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase
    • Gupta SD, Gan K, Schmid MB, Wu HC. 1993. Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase. J. Biol. Chem. 268:16551-56
    • (1993) J. Biol. Chem , vol.268 , pp. 16551-16556
    • Gupta, S.D.1    Gan, K.2    Schmid, M.B.3    Wu, H.C.4
  • 37
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane
    • Harms N, Koningstein G, Dontje W, Muller M, Oudega B, et al. 2001. The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 276:18804-11
    • (2001) J. Biol. Chem , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4    Oudega, B.5
  • 38
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • Hennecke G, Nolte J, Volkmer-Engert R, Schneider-Mergener J, Behrens S. 2005. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J. Biol. Chem. 280:23540-48
    • (2005) J. Biol. Chem , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 40
    • 0022633653 scopus 로고
    • Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membrane and the murein skeleton of the cell envelope
    • Ishidate K, Creeger E, Zrike J, Deb S, Glauner B, et al. 1986. Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membrane and the murein skeleton of the cell envelope. J. Biol. Chem. 261:428-43
    • (1986) J. Biol. Chem , vol.261 , pp. 428-443
    • Ishidate, K.1    Creeger, E.2    Zrike, J.3    Deb, S.4    Glauner, B.5
  • 41
    • 33750454808 scopus 로고    scopus 로고
    • A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins
    • Ito Y, Kanamaru K, Taniguchi N, Miyamoto S, Tokuda H. 2006. A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins. Mol. Microbiol. 62:1064-75
    • (2006) Mol. Microbiol , vol.62 , pp. 1064-1075
    • Ito, Y.1    Kanamaru, K.2    Taniguchi, N.3    Miyamoto, S.4    Tokuda, H.5
  • 42
    • 0010461565 scopus 로고    scopus 로고
    • The assembly pathway of outer membrane protein PhoE of Escherichia coli
    • Jansen C, Heutink M, Tommassen J, de Cock H. 2000. The assembly pathway of outer membrane protein PhoE of Escherichia coli. Eur. J. Biochem. 267:3792-800
    • (2000) Eur. J. Biochem , vol.267 , pp. 3792-3800
    • Jansen, C.1    Heutink, M.2    Tommassen, J.3    de Cock, H.4
  • 44
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice SS, Hunstad DA, Harper JR, Duguay AR, Pinkner JS, et al. 2005. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 187:7680-86
    • (2005) J. Bacteriol , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5
  • 45
    • 4344581281 scopus 로고    scopus 로고
    • Investigation of the structural requirements in the lipopolysaccharide core acceptor for ligation of O antigens in the genus Salmonella: WaaL "ligase" is not the sole determinant of acceptor specificity
    • Kaniuk NA, Vinogradov E, Whitfield C. 2004. Investigation of the structural requirements in the lipopolysaccharide core acceptor for ligation of O antigens in the genus Salmonella: WaaL "ligase" is not the sole determinant of acceptor specificity. J. Biol. Chem. 279:36470-80
    • (2004) J. Biol. Chem , vol.279 , pp. 36470-36480
    • Kaniuk, N.A.1    Vinogradov, E.2    Whitfield, C.3
  • 46
    • 0025314999 scopus 로고
    • The 'Bayer bridges' confronted with results from improved electron microscopy methods
    • Kellenberger E. 1990. The 'Bayer bridges' confronted with results from improved electron microscopy methods. Mol. Microbiol. 4:697-705
    • (1990) Mol. Microbiol , vol.4 , pp. 697-705
    • Kellenberger, E.1
  • 47
    • 0028809455 scopus 로고
    • Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase
    • Kleerebezem M, Heutink M, Tommassen J. 1995. Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase. Mol. Microbiol. 18:313-20
    • (1995) Mol. Microbiol , vol.18 , pp. 313-320
    • Kleerebezem, M.1    Heutink, M.2    Tommassen, J.3
  • 48
    • 0023810885 scopus 로고
    • Internal deletions in the gene for an Escherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide
    • Klose M, Schwarz H, MacIntyre S, Freudl R, Eschbach ML, et al. 1988. Internal deletions in the gene for an Escherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide. J. Biol. Chem. 263:13291-96
    • (1988) J. Biol. Chem , vol.263 , pp. 13291-13296
    • Klose, M.1    Schwarz, H.2    MacIntyre, S.3    Freudl, R.4    Eschbach, M.L.5
  • 49
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik R, Locher KP, Van Gelder P. 2000. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37:239-53
    • (2000) Mol. Microbiol , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 50
    • 0041589300 scopus 로고    scopus 로고
    • Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
    • Kol M, van Dalen A, de Kroon AIPM, de Kruijff B. 2003. Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane. J. Biol. Chem. 278:24586-93
    • (2003) J. Biol. Chem , vol.278 , pp. 24586-24593
    • Kol, M.1    van Dalen, A.2    de Kroon, A.I.P.M.3    de Kruijff, B.4
  • 51
    • 0015969864 scopus 로고
    • Alterations in the outer membrane of the cell envelope of heptose-deficient mutants of Escherichia coli
    • Koplow J, Goldfine H. 1974. Alterations in the outer membrane of the cell envelope of heptose-deficient mutants of Escherichia coli. J. Bacteriol. 181:527-43
    • (1974) J. Bacteriol , vol.181 , pp. 527-543
    • Koplow, J.1    Goldfine, H.2
  • 52
    • 4744373535 scopus 로고    scopus 로고
    • Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite different architecture
    • Korndörfer IP, Dommel MK, Skerra A. 2004. Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite different architecture. Nat. Struct. Mol. Biol. 11:1015-20
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1015-1020
    • Korndörfer, I.P.1    Dommel, M.K.2    Skerra, A.3
  • 53
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V, Sharff A, Koronakis E, Luisi B, Hughes C. 2000. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914-19
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 54
    • 0348093762 scopus 로고    scopus 로고
    • An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane
    • Kozjak V, Wiedemann N, Milenkovic D, Lohaus C, Meyer HE, et al. 2003. An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane. J. Biol. Chem. 278:48520-23
    • (2003) J. Biol. Chem , vol.278 , pp. 48520-48523
    • Kozjak, V.1    Wiedemann, N.2    Milenkovic, D.3    Lohaus, C.4    Meyer, H.E.5
  • 55
    • 0028297759 scopus 로고
    • Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12
    • Laird MW, Kloser AW, Misra R. 1994. Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12. J. Bacteriol. 176:2259-64
    • (1994) J. Bacteriol , vol.176 , pp. 2259-2264
    • Laird, M.W.1    Kloser, A.W.2    Misra, R.3
  • 56
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar SW, Kolter R. 1996. SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178:1770-73
    • (1996) J. Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 58
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, et al. 2006. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol. Microbiol. 61:151-64
    • (2006) Mol. Microbiol , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5
  • 60
    • 0028981022 scopus 로고
    • A novel carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama S, Tajima T, Tokuda H. 1995. A novel carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J. 14:3365-72
    • (1995) EMBO J , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 61
    • 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, Yokota N, Tokuda H. 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. 16:6947-55
    • (1997) EMBO J , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 62
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D, Betton JM, Raina S. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21:871-84
    • (1996) Mol. Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 63
    • 0015830542 scopus 로고
    • Outer membrane of Salmonella. Sites of export of newly synthesised lipopolysaccharide on the bacterial surface
    • Mühlradt PF, Menzel J, Golecki JR, Speth V. 1973. Outer membrane of Salmonella. Sites of export of newly synthesised lipopolysaccharide on the bacterial surface. Eur. J. Biochem. 35:471-81
    • (1973) Eur. J. Biochem , vol.35 , pp. 471-481
    • Mühlradt, P.F.1    Menzel, J.2    Golecki, J.R.3    Speth, V.4
  • 64
  • 65
    • 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. 580:1164-70
    • (2006) FEBS Lett , vol.580 , pp. 1164-1170
    • Narita, S.1    Tokuda, H.2
  • 66
    • 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
  • 69
    • 0346727130 scopus 로고    scopus 로고
    • Evolutionary conservation of biogenesis of β-barrel membrane proteins
    • Paschen SA, Waizenegger T, Stan T, Preuss M, Cyrklaff M, et al. 2003. Evolutionary conservation of biogenesis of β-barrel membrane proteins. Nature 426:862-66
    • (2003) Nature , vol.426 , pp. 862-866
    • Paschen, S.A.1    Waizenegger, T.2    Stan, T.3    Preuss, M.4    Cyrklaff, M.5
  • 71
    • 0033963570 scopus 로고    scopus 로고
    • Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein
    • Prinz T, Tommassen J. 2000. Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein. FEMS Microbiol. Lett. 183:49-53
    • (2000) FEMS Microbiol. Lett , vol.183 , pp. 49-53
    • Prinz, T.1    Tommassen, J.2
  • 72
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley AP. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108
    • (1993) Microbiol. Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 75
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello AE, Harper JR, Silhavy TJ. 2001. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 183:6794-800
    • (2001) J. Bacteriol , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 76
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • Robert V, Volokhina EB, Senf F, Bos MP, Van Gelder P, et al. 2006. Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol. 4:1984-95
    • (2006) PLoS Biol , vol.4 , pp. 1984-1995
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5
  • 77
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière PE, Gross CA. 1996. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:3170-87
    • (1996) Genes Dev , vol.10 , pp. 3170-3187
    • Rouvière, P.E.1    Gross, C.A.2
  • 78
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • Ruiz N, Falcone B, Kahne D, Silhavy TJ. 2005. Chemical conditionality: a genetic strategy to probe organelle assembly. Cell 121:307-17
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 79
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz N, Silhavy TJ. 2005. Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr. Opin. Microbiol. 8:122-26
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 80
    • 0024690869 scopus 로고
    • Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability
    • Sampson BA, Misra R, Benson SA. 1989. Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability. Genetics 122:491-501
    • (1989) Genetics , vol.122 , pp. 491-501
    • Sampson, B.A.1    Misra, R.2    Benson, S.A.3
  • 81
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins
    • Sanchez-Pulido L, Devos D, Genevrois S, Vincente M, Valencia A. 2003. POTRA: a conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins. Trends Biochem. Sci. 28:523-26
    • (2003) Trends Biochem. Sci , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vincente, M.4    Valencia, A.5
  • 82
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran K, Wu HC. 1994. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269:19701-6
    • (1994) J. Biol. Chem , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 83
    • 0025141624 scopus 로고
    • In vivo trimerization of OmpF porin secreted by spheroplasts of Escherichia colt
    • Sen K, Nikaido H. 1990. In vivo trimerization of OmpF porin secreted by spheroplasts of Escherichia colt. Proc. Natl. Acad. Sci. USA 87:743-47
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 743-747
    • Sen, K.1    Nikaido, H.2
  • 84
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
    • Sklar JG, Wu T, Gronenberg LS, Malinverni JC, Kahne D, et al. 2007. Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Proc. Natl. Acad. Sci. USA 104:6400-5
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6400-6405
    • Sklar, J.G.1    Wu, T.2    Gronenberg, L.S.3    Malinverni, J.C.4    Kahne, D.5
  • 85
    • 33845950113 scopus 로고    scopus 로고
    • Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli
    • Sperandeo P, Cescutti R, Villa R, Di Benedetto C, Candia D, et al. 2007. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J. Bacteriol. 189:244-53
    • (2007) J. Bacteriol , vol.189 , pp. 244-253
    • Sperandeo, P.1    Cescutti, R.2    Villa, R.3    Di Benedetto, C.4    Candia, D.5
  • 86
    • 33745974919 scopus 로고    scopus 로고
    • Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus
    • Sperandeo P, Pozzi C, Deho G, Polissi A. 2006. Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus. Res. Microbiol. 157:547-58
    • (2006) Res. Microbiol , vol.157 , pp. 547-558
    • Sperandeo, P.1    Pozzi, C.2    Deho, G.3    Polissi, A.4
  • 87
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spies C, Beil A, Ehrmann M. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-47
    • (1999) Cell , vol.97 , pp. 339-347
    • Spies, C.1    Beil, A.2    Ehrmann, M.3
  • 88
    • 0036740455 scopus 로고    scopus 로고
    • Expression of foreign LpxA acyltransferases in Neisseria meningitidis results in modified lipid A with reduced toxicity and retained adjuvant activity
    • Steeghs L, Berns M, ten Hove J, de Jong A, Roholl P, et al. 2002. Expression of foreign LpxA acyltransferases in Neisseria meningitidis results in modified lipid A with reduced toxicity and retained adjuvant activity. Cell. Microbiol. 4:599-611
    • (2002) Cell. Microbiol , vol.4 , pp. 599-611
    • Steeghs, L.1    Berns, M.2    ten Hove, J.3    de Jong, A.4    Roholl, P.5
  • 89
    • 0037126598 scopus 로고    scopus 로고
    • Outer membrane composition of a lipopolysaccharide-deficient Neisseria meningitidis mutant
    • Steeghs L, de Cock H, Evers E, Zomer B, Tommassen J, et al. 2001. Outer membrane composition of a lipopolysaccharide-deficient Neisseria meningitidis mutant. EMBO J. 20:6937-45
    • (2001) EMBO J , vol.20 , pp. 6937-6945
    • Steeghs, L.1    de Cock, H.2    Evers, E.3    Zomer, B.4    Tommassen, J.5
  • 91
    • 33750287565 scopus 로고    scopus 로고
    • Characterization of pores formed by YaeT (Omp85) from Escherichia coli
    • Stegmeier JF, Andersen C. 2006. Characterization of pores formed by YaeT (Omp85) from Escherichia coli. J. Biochem. 140:275-83
    • (2006) J. Biochem , vol.140 , pp. 275-283
    • Stegmeier, J.F.1    Andersen, C.2
  • 92
    • 33846183762 scopus 로고    scopus 로고
    • Characterization of YtfM, a second member of the Omp85 family in Escherichia coli
    • Stegmeier JF, Glück A, Sukumaran S, Mäntele W, Andersen C. 2007. Characterization of YtfM, a second member of the Omp85 family in Escherichia coli. Biol. Chem. 388:37-46
    • (2007) Biol. Chem , vol.388 , pp. 37-46
    • Stegmeier, J.F.1    Glück, A.2    Sukumaran, S.3    Mäntele, W.4    Andersen, C.5
  • 94
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyvé M, Moons M, Tommassen J. 1991. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J. Mol. Biol. 218:141-48
    • (1991) J. Mol. Biol , vol.218 , pp. 141-148
    • Struyvé, M.1    Moons, M.2    Tommassen, J.3
  • 95
    • 5144228928 scopus 로고    scopus 로고
    • Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution
    • Surana NK, Grass S, Hardy GG, Li H, Thanassi DG, et al. 2004. Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution. Proc. Natl. Acad. Sci. USA 101:14497-503
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14497-14503
    • Surana, N.K.1    Grass, S.2    Hardy, G.G.3    Li, H.4    Thanassi, D.G.5
  • 96
    • 0038602740 scopus 로고    scopus 로고
    • Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
    • Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, et al. 2003. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 22:3199-209
    • (2003) EMBO J , vol.22 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4    Tokuda, H.5
  • 97
    • 14844309359 scopus 로고    scopus 로고
    • E-dependent response of Escherichia coli
    • E-dependent response of Escherichia coli. Mol. Microbiol. 55:1403-12
    • (2005) Mol. Microbiol , vol.55 , pp. 1403-1412
    • Tam, C.1    Missiakas, D.2
  • 98
    • 0035980137 scopus 로고    scopus 로고
    • Structure and assembly of β-barrel membrane proteins
    • Tamm LK, Arora A, Kleinschmidt JH. 2001. Structure and assembly of β-barrel membrane proteins. J. Biol. Chem. 276:32399-402
    • (2001) J. Biol. Chem , vol.276 , pp. 32399-32402
    • Tamm, L.K.1    Arora, A.2    Kleinschmidt, J.H.3
  • 99
    • 27744566698 scopus 로고    scopus 로고
    • MsbA is not required for phospholipid transport in Neisseria meningitidis
    • Tefsen B, Bos MP, Beckers F, Tommassen J, de Cock H. 2005. MsbA is not required for phospholipid transport in Neisseria meningitidis. J. Biol. Chem. 280:35961-66
    • (2005) J. Biol. Chem , vol.280 , pp. 35961-35966
    • Tefsen, B.1    Bos, M.P.2    Beckers, F.3    Tommassen, J.4    de Cock, H.5
  • 100
    • 14244253233 scopus 로고    scopus 로고
    • Lipopolysaccharide transport to the bacterial outer membrane in spheroplasts
    • Tefsen B, Geurtsen J, Beckers F, Tommassen J, de Cock H. 2005. Lipopolysaccharide transport to the bacterial outer membrane in spheroplasts. J. Biol. Chem. 280:4504-9
    • (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
  • 101
    • 0035861554 scopus 로고    scopus 로고
    • Lipoprotein-sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli
    • Terada M, Kuroda T, Matsuyama S, Tokuda H. 2001. Lipoprotein-sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 276:47690-94
    • (2001) J. Biol. Chem , vol.276 , pp. 47690-47694
    • Terada, M.1    Kuroda, T.2    Matsuyama, S.3    Tokuda, H.4
  • 102
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo A, Almirón M, Kolter R. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol. 172:4339-47
    • (1990) J. Bacteriol , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almirón, M.2    Kolter, R.3
  • 104
    • 33644946448 scopus 로고    scopus 로고
    • Protein secretion and secreted proteins in pathogenic Neisseriaceae
    • Van Ulsen P, Tommassen J. 2006. Protein secretion and secreted proteins in pathogenic Neisseriaceae. FEMS Microbiol. Rev. 30:292-319
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 292-319
    • Van Ulsen, P.1    Tommassen, J.2
  • 105
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J. 2003. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299:262-65
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 106
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • Voulhoux R, Tommassen J. 2004. Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly. Res. Microbiol. 155:129-35
    • (2004) Res. Microbiol , vol.155 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 107
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • Waller PR, Sauer RT. 1996. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 178:1146-53
    • (1996) J. Bacteriol , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 108
    • 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 NP, Alba BM, Bose B, Gross CA, Sauer RT. 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
  • 109
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton TA, Sousa MC. 2004. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15:367-74
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 110
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: From siderophores to hemophores
    • Wandersman C, Delepelaire P. 2004. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58:611-47
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 111
    • 0242490833 scopus 로고    scopus 로고
    • Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12
    • Werner J, Augustus AM, Misra R. 2003. Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12. J. Bacteriol. 185:6540-47
    • (2003) J. Bacteriol , vol.185 , pp. 6540-6547
    • Werner, J.1    Augustus, A.M.2    Misra, R.3
  • 112
    • 23844507131 scopus 로고    scopus 로고
    • YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli
    • Werner J, Misra R. 2005. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 57:1450-59
    • (2005) Mol. Microbiol , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 113
    • 0025346393 scopus 로고
    • Stable expression of meningococcal class I protein in an antigenically reactive form in outer membranes of Escherichia coli
    • White DA, Barlow AK, Clarke IN, Heckels JE. 1990. Stable expression of meningococcal class I protein in an antigenically reactive form in outer membranes of Escherichia coli. Mol. Microbiol. 4:769-76
    • (1990) Mol. Microbiol , vol.4 , pp. 769-776
    • White, D.A.1    Barlow, A.K.2    Clarke, I.N.3    Heckels, J.E.4
  • 114
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T, Malinverni J, Ruiz N, Kim S, Silhavy TJ, et al. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235-45
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5
  • 115
    • 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, et al. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 103:11754-59
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5
  • 116
    • 0032524302 scopus 로고    scopus 로고
    • Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis
    • Zhou Z, White K, Polissi A, Georgopoulos C, Raetz CRH. 1998. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 273:12466-75
    • (1998) J. Biol. Chem , vol.273 , pp. 12466-12475
    • Zhou, Z.1    White, K.2    Polissi, A.3    Georgopoulos, C.4    Raetz, C.R.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.