메뉴 건너뛰기




Volumn 140, Issue 2, 2006, Pages 275-283

Characterization of pores formed by YaeT (Omp85) from Escherichia coli

Author keywords

Bacterial outer membrane; Membrane biogenesis; Omp85; Reconstitution in black lipid membranes

Indexed keywords

OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN 85; PERIPLASMIC PROTEIN; PROTEIN YAET; UNCLASSIFIED DRUG;

EID: 33750287565     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj147     Document Type: Article
Times cited : (50)

References (55)
  • 1
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane
    • (Neidhardt, F.C., Curtiss III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., and Magasanik, B., eds.), ASM Press, Washington, DC
    • Nikaido, H. (1996) Outer Membrane. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F.C., Curtiss III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., and Magasanik, B., eds.) pp. 29-47, ASM Press, Washington, DC
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 29-47
    • Nikaido, H.1
  • 2
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge, T.J. (1999) Structures of gram-negative cell walls and their derived membrane vesicles. J. Bacteriol. 181, 4725-4733
    • (1999) J. Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 4
    • 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., and 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, 6947-6955
    • (1997) EMBO J. , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 5
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda, H. and Matsuyama, S. (2004) Sorting of lipoproteins to the outer membrane in E. coli. Biochim. Biophys. Acta 1693, 5-13
    • (2004) Biochim. Biophys. Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 6
    • 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
  • 7
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J.E. and Otzen, D.E. (2005) Interactions between folding factors and bacterial outer membrane proteins. Mol. Microbiol. 57, 326-346
    • (2005) Mol. Microbiol. , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 8
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., Kahne, D., and Silhavy, T.J. (2006) Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 4, 57-66
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 9
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer, U., Beck, K., and Muller, M. (1999) Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274, 24567-24574
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Muller, M.3
  • 10
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris, P.V., Behrens, S., Holst, O., and Kleinschmidt, J.H. (2003) Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 278, 9092-9099
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 11
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A., and Ehrmann, M. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97, 339-347
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 12
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto, H. and Bardwell, J.C. (2004) Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta 1694, 111-119
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.2
  • 13
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S.W. and Kolter, R. (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178, 1770-1773
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 14
    • 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. and 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, 3968-3980
    • (1998) EMBO J. , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 15
    • 0036828872 scopus 로고    scopus 로고
    • PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding
    • Andersen, C., Schiffler, B., Charbit, A., and Benz, R. (2002) PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J. Biol. Chem. 277, 41318-41325
    • (2002) J. Biol. Chem. , vol.277 , pp. 41318-41325
    • Andersen, C.1    Schiffler, B.2    Charbit, A.3    Benz, R.4
  • 16
    • 0041816074 scopus 로고    scopus 로고
    • Probing the orientation of reconstituted maltoporin channels at the single-protein level
    • Danelon, C., Brando, T., and Winterhalter, M. (2003) Probing the orientation of reconstituted maltoporin channels at the single-protein level. J. Biol. Chem. 278, 35542-35551
    • (2003) J. Biol. Chem. , vol.278 , pp. 35542-35551
    • Danelon, C.1    Brando, T.2    Winterhalter, M.3
  • 17
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M.P., Geurtsen, J., Mols, M., and Tommassen, J. (2003) Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299, 262-265
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 18
    • 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., and 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
  • 19
    • 23844507131 scopus 로고    scopus 로고
    • YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli
    • Werner, J. and Misra, R. (2005) YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 57, 1450-1459
    • (2005) Mol. Microbiol. , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 20
    • 23044501295 scopus 로고    scopus 로고
    • Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant
    • Doerrler, W.T. and Raetz, C.R. (2005) Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J. Biol. Chem. 280, 27679-27687
    • (2005) J. Biol. Chem. , vol.280 , pp. 27679-27687
    • Doerrler, W.T.1    Raetz, C.R.2
  • 21
    • 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, T.J., and Kahne, D. (2005) Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121, 235-245
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 22
    • 17444392068 scopus 로고    scopus 로고
    • Characterization of six lipoproteins in the sigmaE regulon
    • Onufryk, C., Crouch, M.L., Fang, F.C., and Gross, C.A. (2005) Characterization of six lipoproteins in the sigmaE regulon. J. Bacteriol. 187, 4552-4561
    • (2005) J. Bacteriol. , vol.187 , pp. 4552-4561
    • Onufryk, C.1    Crouch, M.L.2    Fang, F.C.3    Gross, C.A.4
  • 23
    • 0035028431 scopus 로고    scopus 로고
    • Enhanced expression of the multidrug efflux pumps AcrAB and AcrEF associated with insertion element transposition in Escherichia coli mutants Selected with a fluoroquinolone
    • Jellen-Ritter, A.S. and Kern, W.V. (2001) Enhanced expression of the multidrug efflux pumps AcrAB and AcrEF associated with insertion element transposition in Escherichia coli mutants Selected with a fluoroquinolone. Antimicrob. Agents Chemother. 45, 1467-1472
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1467-1472
    • Jellen-Ritter, A.S.1    Kern, W.V.2
  • 24
    • 0032102987 scopus 로고    scopus 로고
    • Coupling site-directed mutagenesis with high-level expression: Large scale production of mutant porins from E. coli
    • Prilipov, A., Phale, P.S., Van Gelder, P., Rosenbusch, J.P., and Koebnik, R. (1998) Coupling site-directed mutagenesis with high-level expression: large scale production of mutant porins from E. coli. FEMS Microbiol. Lett. 163, 65-72
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 65-72
    • Prilipov, A.1    Phale, P.S.2    Van Gelder, P.3    Rosenbusch, J.P.4    Koebnik, R.5
  • 25
    • 0000768855 scopus 로고    scopus 로고
    • The amplified expression, identification, purification, assay and properties of histidine-tagged bacterial membrane transport proteins
    • (Baldwin, S.A., ed.), Blackwell's Press, Oxford, UK
    • Ward, A., Sanderson, N.M., O'Reilly, J., Rutherford, N.G., Poolman, B., and Henderson, P.J.F. (2000) The amplified expression, identification, purification, assay and properties of histidine-tagged bacterial membrane transport proteins. In: Membrane Transport-A Practical Approach (Baldwin, S.A., ed.) 141-166, Blackwell's Press, Oxford, UK
    • (2000) Membrane Transport - A Practical Approach , pp. 141-166
    • Ward, A.1    Sanderson, N.M.2    O'Reilly, J.3    Rutherford, N.G.4    Poolman, B.5    Henderson, P.J.F.6
  • 26
    • 0018149702 scopus 로고
    • Separation and characterization of the outer membrane of Pseudomonas aeruginosa
    • Mizuno, T. and Kageyama, M. (1978) Separation and characterization of the outer membrane of Pseudomonas aeruginosa. J. Biochem. 84, 179-191
    • (1978) J. Biochem. , vol.84 , pp. 179-191
    • Mizuno, T.1    Kageyama, M.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 29
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., Boos, W., and Läuger, P. (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta 511, 305-319
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4
  • 30
    • 0018378684 scopus 로고
    • Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., and Läuger, P. (1979) Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta 551, 238-247
    • (1979) Biochim. Biophys. Acta , vol.551 , pp. 238-247
    • Benz, R.1    Janko, K.2    Läuger, P.3
  • 31
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A. and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97, 6640-6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 32
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle, I.E., Burri, L., and Lithgow, T. (2005) Molecular architecture and function of the Omp85 family of proteins. Mol. Microbiol. 58, 1216-1225
    • (2005) Mol. Microbiol. , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 33
    • 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
  • 34
    • 0019312556 scopus 로고
    • Major heat-modifiable outer membrane protein in gram-negative bacteria: Comparison with the ompA protein of Escherichia coli
    • Beher, M.G., Schnaitman, C.A., and Pugsley, A.P. (1980) Major heat-modifiable outer membrane protein in gram-negative bacteria: comparison with the ompA protein of Escherichia coli. J. Bacteriol. 143, 906-913
    • (1980) J. Bacteriol. , vol.143 , pp. 906-913
    • Beher, M.G.1    Schnaitman, C.A.2    Pugsley, A.P.3
  • 35
    • 0036926284 scopus 로고    scopus 로고
    • A rapid selective extraction procedure for the outer membrane protein (OmpF) from Escherichia coli
    • Arcidiacono, S., Butler, M.M., Mello, C.M. (2002) A rapid selective extraction procedure for the outer membrane protein (OmpF) from Escherichia coli. Protein Expr. Purif. 25, 134-137
    • (2002) Protein Expr. Purif. , vol.25 , pp. 134-137
    • Arcidiacono, S.1    Butler, M.M.2    Mello, C.M.3
  • 36
    • 0034730655 scopus 로고    scopus 로고
    • Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Guedin, S., Willery, E., Tommassen, J., Fort, E., Drobecq, H., Locht, C., and Jacob-Dubuisson, F. (2000) Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 275, 30202-30210
    • (2000) J. Biol. Chem. , vol.275 , pp. 30202-30210
    • Guedin, S.1    Willery, E.2    Tommassen, J.3    Fort, E.4    Drobecq, H.5    Locht, C.6    Jacob-Dubuisson, F.7
  • 37
    • 0036147641 scopus 로고    scopus 로고
    • Toward genomic identification of beta-barrel membrane proteins: Composition and architecture of known structures
    • Wimley, W.C. (2002) Toward genomic identification of beta-barrel membrane proteins: composition and architecture of known structures. Protein Sci. 11, 301-312
    • (2002) Protein Sci. , vol.11 , pp. 301-312
    • Wimley, W.C.1
  • 40
    • 0032991297 scopus 로고    scopus 로고
    • The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: Determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes
    • Könninger, U.W., Hobbie, S., Benz, R., and Braun, V. (1999) The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes. Mol. Microbiol. 32, 1212-1225
    • (1999) Mol. Microbiol. , vol.32 , pp. 1212-1225
    • Könninger, U.W.1    Hobbie, S.2    Benz, R.3    Braun, V.4
  • 41
    • 0033621401 scopus 로고    scopus 로고
    • Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Jacob-Dubuisson, F., El Hamel, C., Saint, N., Guedin, S., Willery, E., Molle, G., and Locht, C. (1999) Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 274, 37731-37735
    • (1999) J. Biol. Chem. , vol.274 , pp. 37731-37735
    • Jacob-Dubuisson, F.1    El Hamel, C.2    Saint, N.3    Guedin, S.4    Willery, E.5    Molle, G.6    Locht, C.7
  • 43
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah, S.C., Hill, K., Wagner, R., Schlicher, T., and Soll, J. (1997) Reconstitution of a chloroplast protein import channel. EMBO J. 16, 7351-7360
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 44
    • 4043067925 scopus 로고    scopus 로고
    • Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75
    • Tu, S.L., Chen, L.J., Smith, M.D., Su, Y.S., Schnell, D.J., and Li, H.M. (2004) Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75. Plant Cell 16, 2078-2088
    • (2004) Plant Cell , vol.16 , pp. 2078-2088
    • Tu, S.L.1    Chen, L.J.2    Smith, M.D.3    Su, Y.S.4    Schnell, D.J.5    Li, H.M.6
  • 45
    • 23344442676 scopus 로고    scopus 로고
    • The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains
    • Ertel, F., Mirus, O., Bredemeier, R., Moslavac, S., Becker, T., and Schleiff, E. (2005) The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains. J. Biol. Chem. 280, 28281-28289
    • (2005) J. Biol. Chem. , vol.280 , pp. 28281-28289
    • Ertel, F.1    Mirus, O.2    Bredemeier, R.3    Moslavac, S.4    Becker, T.5    Schleiff, E.6
  • 46
    • 33644871665 scopus 로고    scopus 로고
    • Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore
    • Meli, A.C., Hodak, H., Clantin, B., Locht, C., Molle, G., Jacob-Dubuisson, F., and Saint, N. (2006) Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore. J. Biol. Chem. 281, 158-166
    • (2006) J. Biol. Chem. , vol.281 , pp. 158-166
    • Meli, A.C.1    Hodak, H.2    Clantin, B.3    Locht, C.4    Molle, G.5    Jacob-Dubuisson, F.6    Saint, N.7
  • 47
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Muller, D.J. and Engel, A. (1999). Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J. Mol. Biol. 285, 1347-1351
    • (1999) J. Mol. Biol. , vol.285 , pp. 1347-1351
    • Muller, D.J.1    Engel, A.2
  • 48
    • 0036147130 scopus 로고    scopus 로고
    • Electrophysiological behavior of the TolC channel-tunnel in planar lipid bilayers
    • Andersen, C., Hughes, C., and Koronakis, V. (2002). Electrophysiological behavior of the TolC channel-tunnel in planar lipid bilayers. J. Membr. Biol. 185, 83-92
    • (2002) J. Membr. Biol. , vol.185 , pp. 83-92
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 49
    • 0023783439 scopus 로고
    • Permeation of hydrophilic molecules through the outer membrane of gram-negative bacteria. Review on bacterial porins
    • Benz, R. and Bauer, K. (1988) Permeation of hydrophilic molecules through the outer membrane of gram-negative bacteria. Review on bacterial porins. Eur. J. Biochem. 176, 1-19
    • (1988) Eur. J. Biochem. , vol.176 , pp. 1-19
    • Benz, R.1    Bauer, K.2
  • 50
    • 0032970556 scopus 로고    scopus 로고
    • In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: Contribution to maltose and maltooligosaccharide transport and binding
    • Andersen, C., Bachmeyer, C., Täuber, H., Benz, R., Wang, J., Michel, V., Newton, S.M., Hofnung, M., and Charbit, A. (1999) In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding. Mol. Microbiol. 32, 851-867
    • (1999) Mol. Microbiol. , vol.32 , pp. 851-867
    • Andersen, C.1    Bachmeyer, C.2    Täuber, H.3    Benz, R.4    Wang, J.5    Michel, V.6    Newton, S.M.7    Hofnung, M.8    Charbit, A.9
  • 52
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sanchez-Pulido, L., Devos, D., Genevrois, S., Vicente, M., and Valencia, A. (2003) POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 28, 523-526
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 53
    • 0033777399 scopus 로고    scopus 로고
    • ShlB mutants of Serratia marcescens allow uncoupling of activation and secretion of the ShlA hemolysin
    • Yang, F.L. and Braun, V. (2000) ShlB mutants of Serratia marcescens allow uncoupling of activation and secretion of the ShlA hemolysin. Int. J. Med. Microbiol. 290, 529-538
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 529-538
    • Yang, F.L.1    Braun, V.2
  • 54
    • 0030047151 scopus 로고    scopus 로고
    • The permeability of the wall fabric of Escherichia coli and Bacillus subtilis
    • Demchick, P. and Koch, A.L. (1996) The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J. Bacteriol. 178, 768-773
    • (1996) J. Bacteriol. , vol.178 , pp. 768-773
    • Demchick, P.1    Koch, A.L.2
  • 55
    • 0033813837 scopus 로고    scopus 로고
    • On the architecture of the gram-negative bacterial murein sacculus
    • Pink, D., Moeller, J., Quinn, B., Jericho, M., and Beveridge, T. (2000) On the architecture of the gram-negative bacterial murein sacculus. J. Bacteriol. 182, 5925-5930
    • (2000) J. Bacteriol. , vol.182 , pp. 5925-5930
    • Pink, D.1    Moeller, J.2    Quinn, B.3    Jericho, M.4    Beveridge, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.