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Volumn 35, Issue 4, 2000, Pages 777-790

In vivo and in vitro studies of transmembrane β-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; MALTOPORIN; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; PORIN; UNCLASSIFIED DRUG;

EID: 0033982057     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01748.x     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 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., et al. (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
  • 2
    • 0028926959 scopus 로고
    • Evaluation of the rate constants of sugar transport through maltoprin (LamB) of Escherichia coli from the sugar-induced current noise
    • Andersen, C., Jordy, M., and Benz, R. (1995) Evaluation of the rate constants of sugar transport through maltoprin (LamB) of Escherichia coli from the sugar-induced current noise. J Gen Physiol 105: 385-401.
    • (1995) J Gen Physiol , vol.105 , pp. 385-401
    • Andersen, C.1    Jordy, M.2    Benz, R.3
  • 3
    • 0032146885 scopus 로고    scopus 로고
    • Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis
    • Andersen, C., Cseh, R., Schülein, K., and Benz, R. (1998) Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis. J Membr Biol 164: 263-274.
    • (1998) J Membr Biol , vol.164 , pp. 263-274
    • Andersen, C.1    Cseh, R.2    Schülein, K.3    Benz, R.4
  • 5
    • 33645607378 scopus 로고
    • Solute uptake through bacterial outer membranes
    • Hackenbek, R., and Ghuysen, J.-M. (eds). Amsterdam: Elsevier
    • Benz, R. (1994) Solute uptake through bacterial outer membranes. In Bacterial Cell Wall, Vol. 27. Hackenbek, R., and Ghuysen, J.-M. (eds). Amsterdam: Elsevier, pp. 397-423.
    • (1994) Bacterial Cell Wall , vol.27 , pp. 397-423
    • Benz, R.1
  • 6
    • 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
  • 7
    • 0022515322 scopus 로고
    • Pore formation by LamB of E. coli in lipid bilayer membranes
    • Benz, R., Schmid, A., Nakae, T., and Vos-Scheperkeuter, G.H. (1986) Pore formation by LamB of E. coli in lipid bilayer membranes. J Bacteriol 165: 978-986.
    • (1986) J Bacteriol , vol.165 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scheperkeuter, G.H.4
  • 8
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane
    • Benz, R., Schmid, A., and Vos-Scheperkeuter, G. (1987) Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J Membr Biol 100: 12-29.
    • (1987) J Membr Biol , vol.100 , pp. 12-29
    • Benz, R.1    Schmid, A.2    Vos-Scheperkeuter, G.3
  • 9
    • 0024549961 scopus 로고
    • Molecular basis of porin selectivity: Membrane experiments with OmpC-PhoE and OmpF-PhoE hybrid proteins of Escherichia coli K-12
    • Benz, R., Schmid, A., Van der Ley, P., and Tommassen, J. (1989) Molecular basis of porin selectivity: membrane experiments with OmpC-PhoE and OmpF-PhoE hybrid proteins of Escherichia coli K-12. Biochim Biophys Acta 981: 8-14.
    • (1989) Biochim Biophys Acta , vol.981 , pp. 8-14
    • Benz, R.1    Schmid, A.2    Van Der Ley, P.3    Tommassen, J.4
  • 10
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins: Mutations changing the maltodextrin binding site
    • Benz, R., Francis, G., Nakae, T., and Ferenci, T. (1992) Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site. Biochim Biophys Acta 1104: 299-307.
    • (1992) Biochim Biophys Acta , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 11
    • 0030595346 scopus 로고    scopus 로고
    • Probing the structural role of an β loop of maltose-binding protein by mutagenesis: Heat shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies
    • Betton, J.M., Boscus, D., Missiakas, S.R., and Hofnung, M. (1996) Probing the structural role of an β loop of maltose-binding protein by mutagenesis: heat shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J Mol Biol 262: 140-150.
    • (1996) J Mol Biol , vol.262 , pp. 140-150
    • Betton, J.M.1    Boscus, D.2    Missiakas, S.R.3    Hofnung, M.4
  • 12
    • 0022911351 scopus 로고
    • Mutagenesis by random linker insertion into the lamB gene of E. coli K12
    • Boulain, J.C., Charbit, A., and Hofnung, M. (1986) Mutagenesis by random linker insertion into the lamB gene of E. coli K12. Mol Gen Genet 205: 339-348.
    • (1986) Mol Gen Genet , vol.205 , pp. 339-348
    • Boulain, J.C.1    Charbit, A.2    Hofnung, M.3
  • 13
    • 0019845615 scopus 로고
    • In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K12
    • Braun-Breton, C., and Hofnung, M. (1981) In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K12. J Bacteriol 148: 845-852.
    • (1981) J Bacteriol , vol.148 , pp. 845-852
    • Braun-Breton, C.1    Hofnung, M.2
  • 14
    • 0032900438 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane active transporter FepA from Escherichia coli
    • Buchanan, S., Smith, B., Venkatramani, L., Xia, D., Esser, L., Palnitkar, M., ef al. (1999) Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nature Struct Biol 6: 56-63.
    • (1999) Nature Struct Biol , vol.6 , pp. 56-63
    • Buchanan, S.1    Smith, B.2    Venkatramani, L.3    Xia, D.4    Esser, L.5    Palnitkar, M.6
  • 15
    • 0021982912 scopus 로고
    • Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K12
    • Charbit, A., and Hofnung, M. (1985) Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K12. J Virol 53: 667-671.
    • (1985) J Virol , vol.53 , pp. 667-671
    • Charbit, A.1    Hofnung, M.2
  • 16
    • 0022814620 scopus 로고
    • Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope: Expression at the cell surface
    • Charbit, A., Boulain, J.C., Ryter, A., and Hofnung, M. (1986) Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope: expression at the cell surface. EMBO J 5: 3029-3037.
    • (1986) EMBO J , vol.5 , pp. 3029-3037
    • Charbit, A.1    Boulain, J.C.2    Ryter, A.3    Hofnung, M.4
  • 17
    • 0024278661 scopus 로고
    • Maltose transport and starch binding in phage resistant point mutants of maltoporin functional and topological implications
    • Charbit, A., Gehring, K., Nikaido, H., Ferenci, T., and Hofnung, M. (1988) Maltose transport and starch binding in phage resistant point mutants of maltoporin functional and topological implications. J Mol Biol 201: 487-496.
    • (1988) J Mol Biol , vol.201 , pp. 487-496
    • Charbit, A.1    Gehring, K.2    Nikaido, H.3    Ferenci, T.4    Hofnung, M.5
  • 18
    • 0025958720 scopus 로고
    • Permissive sites and the topology of an outer-membrane protein with a reporter epitope
    • Charbit, A., Ronco, J., Michel, V., Werts, C., and Hofnung, M. (1991) Permissive sites and the topology of an outer-membrane protein with a reporter epitope. J Bacteriol 173: 262-275.
    • (1991) J Bacteriol , vol.173 , pp. 262-275
    • Charbit, A.1    Ronco, J.2    Michel, V.3    Werts, C.4    Hofnung, M.5
  • 19
    • 0028277842 scopus 로고
    • A role of residue 151 of LamB in bacteriophage lambda adsorption: Possible steric effect of amino acid substitutions
    • Charbit, A., Werts, C., Michel, V., Klebba, P.E., Quillardet, P., and Hofnung, M. (1994) A role of residue 151 of LamB in bacteriophage lambda adsorption: possible steric effect of amino acid substitutions. J Bacteriol 176: 3204-3209.
    • (1994) J Bacteriol , vol.176 , pp. 3204-3209
    • Charbit, A.1    Werts, C.2    Michel, V.3    Klebba, P.E.4    Quillardet, P.5    Hofnung, M.6
  • 20
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., et al. (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358: 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3    Steiert, M.4    Ghosh, R.5    Pauptit, R.A.6
  • 21
    • 0022727889 scopus 로고
    • Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli
    • Desaymard, C., Debarbouillé, M., Jolit, M., and Schwartz, M. (1986) Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli. EMBO J 5: 1383-1388.
    • (1986) EMBO J , vol.5 , pp. 1383-1388
    • Desaymard, C.1    Debarbouillé, M.2    Jolit, M.3    Schwartz, M.4
  • 22
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Wang, Y.F., Rizkallah, P., Rosenbusch, J.P., and Schirmer, T. (1996) Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4: 127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 23
    • 0019254027 scopus 로고
    • The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins
    • Ferenci, T., and Boos, W. (1980) The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins. J Supramol Struct 13: 101-116.
    • (1980) J Supramol Struct , vol.13 , pp. 101-116
    • Ferenci, T.1    Boos, W.2
  • 24
    • 0020491174 scopus 로고
    • Directed evolution of the lambda receptor of Escherichia coli through affinity chromotography selection
    • Ferenci, T., and Lee, K.S. (1982) Directed evolution of the lambda receptor of Escherichia coli through affinity chromotography selection. J Mol Biol 160: 431-444.
    • (1982) J Mol Biol , vol.160 , pp. 431-444
    • Ferenci, T.1    Lee, K.S.2
  • 25
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A., Hofmann, E., Coulton, J., Diederichs, K., and Weite, W. (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282: 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.1    Hofmann, E.2    Coulton, J.3    Diederichs, K.4    Weite, W.5
  • 26
    • 0027471832 scopus 로고
    • Crystallization and preliminary X-ray analysis of ScrY, a specific bacterial outer membrane porin
    • Forst, D., Schülein, K., Wacker, T., Kreutz, W., Benz, R., and Weite, W. (1993) Crystallization and preliminary X-ray analysis of ScrY, a specific bacterial outer membrane porin. J Mol Biol 229: 258-262.
    • (1993) J Mol Biol , vol.229 , pp. 258-262
    • Forst, D.1    Schülein, K.2    Wacker, T.3    Kreutz, W.4    Benz, R.5    Weite, W.6
  • 27
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst, D., Welte, W., Wacker, T., and Diederichs, K. (1998) Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Struct Biol 5: 37-46.
    • (1998) Nature Struct Biol , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 28
    • 0025912181 scopus 로고
    • Affinity-chromatographic purification of sixteen cysteine-substituted maltoporin variants: Thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli
    • Francis, G., Brennan, L., and Ferenci, T. (1991) Affinity-Chromatographic purification of sixteen cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli. Biochim Biophys Acta 1067: 89-96.
    • (1991) Biochim Biophys Acta , vol.1067 , pp. 89-96
    • Francis, G.1    Brennan, L.2    Ferenci, T.3
  • 29
    • 0023906938 scopus 로고
    • Facilitated diffusion of p-nitrophenyl-α-d-maltohexaoside through the outer membrane of Escherichia coli
    • Freundlieb, S., Ehmann, U., and Boos, W. (1988) Facilitated diffusion of p-nitrophenyl-α-d-maltohexaoside through the outer membrane of Escherichia coli. J Biol Chem 263: 314-320.
    • (1988) J Biol Chem , vol.263 , pp. 314-320
    • Freundlieb, S.1    Ehmann, U.2    Boos, W.3
  • 30
    • 0020318345 scopus 로고
    • Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein
    • Gabay, J., and Schwarte, M. (1982) Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein. J Biol Chem 257: 6627-6630.
    • (1982) J Biol Chem , vol.257 , pp. 6627-6630
    • Gabay, J.1    Schwarte, M.2
  • 31
    • 0031058792 scopus 로고    scopus 로고
    • The structure of porin from Paracoccus denitrificans at 3.1 å resolution
    • Hirsch, A., Diederichs, K., Breed, J., Saxena, K., Richter, O.M., Ludwig, B., e al. (1997) The structure of porin from Paracoccus denitrificans at 3.1 Å resolution. FEBS Lett 404: 208-210.
    • (1997) FEBS Lett , vol.404 , pp. 208-210
    • Hirsch, A.1    Diederichs, K.2    Breed, J.3    Saxena, K.4    Richter, O.M.5    Ludwig, B.6
  • 32
    • 0028933982 scopus 로고
    • An intelligent channel
    • Hofnung, M. (1995) An intelligent channel (and more). Science 267: 473-474.
    • (1995) Science , vol.267 , pp. 473-474
    • Hofnung, M.1
  • 33
    • 0030596521 scopus 로고    scopus 로고
    • Rate constants of sugar transport through two LamB mutants of Escherichia coli: Comparison with wild-type maltoporin and LamB of Salmonella typhimurium
    • Jordy, M., Andersen, C., Schulein, K., Ferenci, T., and Benz, R. (1996) Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and LamB of Salmonella typhimurium. J Mol Biol 259: 666-678.
    • (1996) J Mol Biol , vol.259 , pp. 666-678
    • Jordy, M.1    Andersen, C.2    Schulein, K.3    Ferenci, T.4    Benz, R.5
  • 34
    • 0027959128 scopus 로고
    • A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis
    • Klebba, P., Hofnung, M., and Charbit, A. (1994) A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J 13: 4670-4675.
    • (1994) EMBO J , vol.13 , pp. 4670-4675
    • Klebba, P.1    Hofnung, M.2    Charbit, A.3
  • 35
    • 0025942159 scopus 로고
    • Deletions or duplications in the BtuB protein affect its level in the outer membrane of Escherichia coli
    • Koster, W., Gudmundsdottir, A., Lundrigan, M., Seiffert, A., and Kadner, R. (1991) Deletions or duplications in the BtuB protein affect its level in the outer membrane of Escherichia coli. J Bacteriol 173: 5639-5647.
    • (1991) J Bacteriol , vol.173 , pp. 5639-5647
    • Koster, W.1    Gudmundsdottir, A.2    Lundrigan, M.3    Seiffert, A.4    Kadner, R.5
  • 36
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomas blastica at 2.0 Å resolution
    • Kreusch, A., Neubüser, A., Schiltz, E., Weckesser, J., and Schulz, G.E. (1994) Structure of the membrane channel porin from Rhodopseudomas blastica at 2.0 Å resolution. Protein Sci 3: 58-63.
    • (1994) Protein Sci , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubüser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 37
    • 0023429366 scopus 로고
    • Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes
    • van der Ley, P., Burm, P., Agterberg, M., van Meersbergen, J., and Tommassen, J. (1987) Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes. Mol Gen Genet 209: 585-591.
    • (1987) Mol Gen Genet , vol.209 , pp. 585-591
    • Ley, P.1    Burm, P.2    Agterberg, M.3    Van Meersbergen, J.4    Tommassen, J.5
  • 38
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer, J.E.W., Hofnung, M., and Schulz, G.E. (1997) Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol 266: 761-775.
    • (1997) J Mol Biol , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 39
    • 0002972659 scopus 로고
    • Unit VII. Assays of the lac operon enzymes
    • Miller, J.H. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Unit VII. Assays of the lac operon enzymes. In Experiments in Molecular Genetics. Miller, J.H. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 352-355.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 40
    • 0028266944 scopus 로고
    • Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: Evaluation of the sugar binding kinetics to the channel interior
    • Nekolla, S., Andersen, C., and Benz, R. (1994) Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: evaluation of the sugar binding kinetics to the channel interior. Biophys J 86: 1388-1397.
    • (1994) Biophys J , vol.86 , pp. 1388-1397
    • Nekolla, S.1    Andersen, C.2    Benz, R.3
  • 41
    • 0029971104 scopus 로고    scopus 로고
    • Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model
    • Newton, S.M.C., Klebba, P.E., Michel, V., Hofnung, M., and Charbit, A. (1996) Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J Bacteriol 178: 3447-3456.
    • (1996) J Bacteriol , vol.178 , pp. 3447-3456
    • Newton, S.M.C.1    Klebba, P.E.2    Michel, V.3    Hofnung, M.4    Charbit, A.5
  • 42
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability. FEMS Microbiol Rev 49: 1-32.
    • (1985) FEMS Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 43
    • 0028920231 scopus 로고
    • The rpoE gene encoding the σE (σ24) heat shock sigma factor of Escherichia coli
    • Raina, S., Missiakas, D., and Georgopoulos, C. (1995) The rpoE gene encoding the σE (σ24) heat shock sigma factor of Escherichia coli. EMBO J 14: 1043-1055.
    • (1995) EMBO J , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 44
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution
    • Schirmer, T., Keller, T., Wang, Y.F., and Rosenbush, J.P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution. Science 267: 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.2    Wang, Y.F.3    Rosenbush, J.P.4
  • 45
    • 0025869336 scopus 로고
    • A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria
    • Schmid, K., Ebner, R., Jahreis, K., Lengeler, J.W., and Titgemeyer, F. (1991) A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria. Mol Microbiol 5: 941-950.
    • (1991) Mol Microbiol , vol.5 , pp. 941-950
    • Schmid, K.1    Ebner, R.2    Jahreis, K.3    Lengeler, J.W.4    Titgemeyer, F.5
  • 46
    • 0025893079 scopus 로고
    • The sugar-specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins
    • Schülein, K., Schmid, K., and Benz, R. (1991) The sugar-specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins. Mol Microbiol 5: 2233-2241.
    • (1991) Mol Microbiol , vol.5 , pp. 2233-2241
    • Schülein, K.1    Schmid, K.2    Benz, R.3
  • 47
    • 0016678144 scopus 로고
    • Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor
    • Szmelcman, S., and Hofnung, M. (1975) Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor. J Bacteriol 124: 112-118.
    • (1975) J Bacteriol , vol.124 , pp. 112-118
    • Szmelcman, S.1    Hofnung, M.2
  • 48
    • 0026096589 scopus 로고
    • The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution
    • Weiss, M.S., Kreusch, A., Schiltz, E., Nestel, U., Welte, W., Weckesser, J., et al. (1991) The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Lett 280: 379-382.
    • (1991) FEBS Lett , vol.280 , pp. 379-382
    • Weiss, M.S.1    Kreusch, A.2    Schiltz, E.3    Nestel, U.4    Welte, W.5    Weckesser, J.6
  • 49
    • 0028029005 scopus 로고
    • Adsorption of bacteriophage lambda on the LamB protein of E. coli K12: Point mutations in gene J of lambda responsible for extended host range
    • Werts, C., Michel, V., Hofnung, M., and Charbit, A. (1994) Adsorption of bacteriophage lambda on the LamB protein of E. coli K12: point mutations in gene J of lambda responsible for extended host range. J Bacteriol 176: 941-947.
    • (1994) J Bacteriol , vol.176 , pp. 941-947
    • Werts, C.1    Michel, V.2    Hofnung, M.3    Charbit, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.