메뉴 건너뛰기




Volumn 153, Issue 7, 2002, Pages 417-424

Mechanism of maltodextrin transport through LamB

Author keywords

LamB; Maltodextrin; Maltoporins; Transport

Indexed keywords

AROMATIC AMINO ACID; CARRIER PROTEIN; MALTODEXTRIN; PORIN; PROTEIN LAMB; UNCLASSIFIED DRUG;

EID: 0036034187     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-2508(02)01340-2     Document Type: Conference Paper
Times cited : (28)

References (62)
  • 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
    • In Process Citation
    • Andersen C., Bachmeyer C., Tauber H., Benz R., Wang J., Michel V., Newton S.M., Hofnung M., Charbit A. 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. 32:1999;851-867. [In Process Citation].
    • (1999) Mol. Microbiol. , vol.32 , pp. 851-867
    • Andersen, C.1    Bachmeyer, C.2    Tauber, H.3    Benz, R.4    Wang, J.5    Michel, V.6    Newton, S.M.7    Hofnung, M.8    Charbit, A.9
  • 2
    • 0017648838 scopus 로고
    • Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein
    • Bavoil P., Nikaido H., von Meyenburg K. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol. Gen. Genet. 158:1977;23-33.
    • (1977) Mol. Gen. Genet. , vol.158 , pp. 23-33
    • Bavoil, P.1    Nikaido, H.2    Von Meyenburg, K.3
  • 3
    • 0026318173 scopus 로고
    • Zones of membrane adhesion in the cryofixed envelope of Escherichia coli
    • Bayer M.E. Zones of membrane adhesion in the cryofixed envelope of Escherichia coli. J. Struct. Biol. 107:1991;268-280.
    • (1991) J. Struct. Biol. , vol.107 , pp. 268-280
    • Bayer, M.E.1
  • 4
    • 0024119777 scopus 로고
    • The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis
    • Bolla J.M., Lazdunski C., Pages J.M. The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis. EMBO J. 7:1988;3595-3599.
    • (1988) EMBO J. , vol.7 , pp. 3595-3599
    • Bolla, J.M.1    Lazdunski, C.2    Pages, J.M.3
  • 5
    • 0021315388 scopus 로고
    • Linker mutagenesis in the gene of an outer membrane protein of Escherichia coli, lamB
    • Bouges-Bocquet B., Villarroya H., Hofnung M. Linker mutagenesis in the gene of an outer membrane protein of Escherichia coli, lamB. J. Cell. Biochem. 24:1984;217-228.
    • (1984) J. Cell. Biochem. , vol.24 , pp. 217-228
    • Bouges-Bocquet, B.1    Villarroya, H.2    Hofnung, M.3
  • 6
    • 0017103909 scopus 로고
    • Transport of vitamin B12 in Escherichia coli: Energy dependence
    • Bradbeer C., Woodrow M.L. Transport of vitamin B12 in Escherichia coli: Energy dependence. J. Bacteriol. 128:1976;99-104.
    • (1976) J. Bacteriol. , vol.128 , pp. 99-104
    • Bradbeer, C.1    Woodrow, M.L.2
  • 7
    • 0019845615 scopus 로고
    • In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K-12
    • Braun-Breton C., Hofnung M. In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K-12. J. Bacteriol. 148:1981;845-852.
    • (1981) J. Bacteriol. , vol.148 , pp. 845-852
    • Braun-Breton, C.1    Hofnung, M.2
  • 9
    • 0033982057 scopus 로고    scopus 로고
    • In vivo and in vitro studies of transmembrane beta-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin
    • Charbit A., Andersen C., Wang J., Schiffler B., Michel V., Benz R., Hofnung M. In vivo and in vitro studies of transmembrane beta-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin. Mol. Microbiol. 35:2000;777-790.
    • (2000) Mol. Microbiol. , vol.35 , pp. 777-790
    • Charbit, A.1    Andersen, C.2    Wang, J.3    Schiffler, B.4    Michel, V.5    Benz, R.6    Hofnung, M.7
  • 10
    • 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., Hofnung M. Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope expression at the cell surface. EMBO J. 5:1986;3029-3037.
    • (1986) EMBO J. , vol.5 , pp. 3029-3037
    • Charbit, A.1    Boulain, J.C.2    Ryter, A.3    Hofnung, M.4
  • 11
    • 0021770587 scopus 로고
    • Further sequence analysis of the phage lambda receptor site. Possible implications for the organization of the lamB protein in Escherichia coli K12
    • Charbit A., Clement J.M., Hofnung M. Further sequence analysis of the phage lambda receptor site. Possible implications for the organization of the lamB protein in Escherichia coli K12. J. Mol. Biol. 175:1984;395-401.
    • (1984) J. Mol. Biol. , vol.175 , pp. 395-401
    • Charbit, A.1    Clement, J.M.2    Hofnung, M.3
  • 12
    • 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., Hofnung M. Maltose transport and starch binding in phage-resistant point mutants of maltoporin. Functional and topological implications. J. Mol. Biol. 201:1988;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
  • 13
    • 0021982912 scopus 로고
    • Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K-12
    • Charbit A., Hofnung M. Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K-12. J. Virol. 53:1985;667-671.
    • (1985) J. Virol. , vol.53 , pp. 667-671
    • Charbit, A.1    Hofnung, M.2
  • 14
    • 0031736256 scopus 로고    scopus 로고
    • A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake
    • Charbit A., Wang J., Michel V., Hofnung M. A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake. Mol. Gen. Genet. 260:1998;185-192.
    • (1998) Mol. Gen. Genet. , vol.260 , pp. 185-192
    • Charbit, A.1    Wang, J.2    Michel, V.3    Hofnung, M.4
  • 15
    • 0019856948 scopus 로고
    • Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12
    • Clement J.M., Hofnung M. Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell. 27:1981;507-514.
    • (1981) Cell , vol.27 , pp. 507-514
    • Clement, J.M.1    Hofnung, M.2
  • 17
    • 0024278648 scopus 로고
    • Effect of point mutations on the in vitro pore properties of maltoporin, a protein of Escherichia coli outer membrane
    • Dargent B., Charbit A., Hofnung M., Pattus F. Effect of point mutations on the in vitro pore properties of maltoporin, a protein of Escherichia coli outer membrane. J. Mol. Biol. 201:1988;497-506.
    • (1988) J. Mol. Biol. , vol.201 , pp. 497-506
    • Dargent, B.1    Charbit, A.2    Hofnung, M.3    Pattus, F.4
  • 18
    • 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. Lipopolysaccharides and divalent cations are involved in the formation of an assembly-competent intermediate of outer-membrane protein PhoE of E. coli. EMBO J. 15:1996;5567-5573.
    • (1996) EMBO J. , vol.15 , pp. 5567-5573
    • De Cock, H.1    Tommassen, J.2
  • 19
    • 0017109844 scopus 로고
    • Outer membrane of Gram-negative bacteria. XII. Molecular-sieving function of cell wall
    • Decad G.M., Nikaido H. Outer membrane of Gram-negative bacteria. XII. Molecular-sieving function of cell wall. J. Bacteriol. 128:1976;325-336.
    • (1976) J. Bacteriol. , vol.128 , pp. 325-336
    • Decad, G.M.1    Nikaido, H.2
  • 20
    • 0015694445 scopus 로고
    • Transport of vitamin B12 in Escherichia coli: Common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope
    • Di Masi D.R., White J.C., Schnaitman C.A., Bradbeer C. Transport of vitamin B12 in Escherichia coli: Common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope. J. Bacteriol. 115:1973;506-513.
    • (1973) J. Bacteriol. , vol.115 , pp. 506-513
    • Di Masi, D.R.1    White, J.C.2    Schnaitman, C.A.3    Bradbeer, C.4
  • 21
    • 0037154084 scopus 로고    scopus 로고
    • Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands
    • Duan X., Quiocho F.A. Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands. Biochemistry. 41:2002;706-712.
    • (2002) Biochemistry , vol.41 , pp. 706-712
    • Duan, X.1    Quiocho, F.A.2
  • 23
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide [see comments]
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide [see comments]. Science. 282:1998;2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 24
    • 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., Diederichs K. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. [see comments] Nat. Struct. Biol. 5:1998;37-46.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 25
    • 0023182756 scopus 로고
    • Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein
    • Gehring K., Charbit A., Brissaud E., Hofnung M. Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein. J. Bacteriol. 169:1987;2103-2106.
    • (1987) J. Bacteriol. , vol.169 , pp. 2103-2106
    • Gehring, K.1    Charbit, A.2    Brissaud, E.3    Hofnung, M.4
  • 26
    • 0018892680 scopus 로고
    • DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory protein
    • Hedgpeth J., Clement J.M., Marchal C., Perrin D., Hofnung M. DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory protein. Proc. Natl. Acad. Sci. USA. 77:1980;2621-2625.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2621-2625
    • Hedgpeth, J.1    Clement, J.M.2    Marchal, C.3    Perrin, D.4    Hofnung, M.5
  • 27
    • 0015969332 scopus 로고
    • MalB region in Escherichia coli K-12: Characterization of new mutations
    • Hofnung M., Hatfield D., Schwartz M. malB region in Escherichia coli K-12: Characterization of new mutations. J. Bacteriol. 117:1974;40-47.
    • (1974) J. Bacteriol. , vol.117 , pp. 40-47
    • Hofnung, M.1    Hatfield, D.2    Schwartz, M.3
  • 28
    • 0015171906 scopus 로고
    • Mutations allowing growth on maltose of Escherichia coli K12 strains with a deleted malT gene
    • Hofnung M., Schwartz M. Mutations allowing growth on maltose of Escherichia coli K12 strains with a deleted malT gene. Mol. Gen. Genet. 112:1971;117-132.
    • (1971) Mol. Gen. Genet. , vol.112 , pp. 117-132
    • Hofnung, M.1    Schwartz, M.2
  • 29
    • 0015223531 scopus 로고
    • Complementation studies in the maltose-A region of the Escherichia coli K12 genetic map
    • Hofnung M., Schwartz M., Hatfield D. Complementation studies in the maltose-A region of the Escherichia coli K12 genetic map. J. Mol. Biol. 61:1971;681-694.
    • (1971) J. Mol. Biol. , vol.61 , pp. 681-694
    • Hofnung, M.1    Schwartz, M.2    Hatfield, D.3
  • 30
    • 0027959128 scopus 로고
    • A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis
    • Klebba P.E., Hofnung M., Charbit A. A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J. 13:1994;4670-4675.
    • (1994) EMBO J. , vol.13 , pp. 4670-4675
    • Klebba, P.E.1    Hofnung, M.2    Charbit, A.3
  • 31
    • 0032034801 scopus 로고    scopus 로고
    • Mechanisms of solute transport through outer membrane porins: Burning down the house
    • Klebba P.E., Newton S.M. Mechanisms of solute transport through outer membrane porins: Burning down the house. Curr. Opin. Microbiol. 1:1998;238-247.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 238-247
    • Klebba, P.E.1    Newton, S.M.2
  • 32
    • 0030871753 scopus 로고    scopus 로고
    • Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin
    • Klebba P.E., Newton S.M., Charbit A., Michel V., Perrin D., Hofnung M. Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin. Res. Microbiol. 148:1997;375-387.
    • (1997) Res. Microbiol. , vol.148 , pp. 375-387
    • Klebba, P.E.1    Newton, S.M.2    Charbit, A.3    Michel, V.4    Perrin, D.5    Hofnung, M.6
  • 33
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 A resolution
    • Kreusch A., Neubuser A., Schiltz E., Weckesser J., Schulz G.E. Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 A resolution. Protein Sci. 3:1994;58-63.
    • (1994) Protein Sci. , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubuser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 34
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J.P., Moras D. Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 95:1998;771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 35
    • 0018824608 scopus 로고
    • Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: Inhibition by higher oligosaccharides of maltose series
    • Luckey M., Nikaido H. Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: Inhibition by higher oligosaccharides of maltose series. Biochem. Biophys. Res. Commun. 93:1980;166-171.
    • (1980) Biochem. Biophys. Res. Commun. , vol.93 , pp. 166-171
    • Luckey, M.1    Nikaido, H.2
  • 36
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli
    • Luckey M., Nikaido H. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc. Natl. Acad. Sci. USA. 77:1980;167-171.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 167-171
    • Luckey, M.1    Nikaido, H.2
  • 37
    • 0020351713 scopus 로고
    • Mutations in gene lamB: Studies on structure and topology of an E. coli outer membrane protein Tokai
    • Marchal C., Clement J.M., Hofnung M. Mutations in gene lamB: Studies on structure and topology of an E. coli outer membrane protein Tokai. J. Exp. Clin. Med. 7:1982;165-170.
    • (1982) J. Exp. Clin. Med. , vol.7 , pp. 165-170
    • Marchal, C.1    Clement, J.M.2    Hofnung, M.3
  • 38
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer J.E., Hofnung M., Schulz G.E. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266:1997;761-775.
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.1    Hofnung, M.2    Schulz, G.E.3
  • 39
    • 0030902082 scopus 로고    scopus 로고
    • Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions
    • Meyer J.E., Schulz G.E. Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions. Protein Sci. 6:1997;1084-1091.
    • (1997) Protein Sci. , vol.6 , pp. 1084-1091
    • Meyer, J.E.1    Schulz, G.E.2
  • 40
    • 0024426707 scopus 로고
    • Antibodies against synthetic peptides and the topology of LamB, an outer membrane protein from Escherichia coli K12
    • Molla A., Charbit A., Le Guern A., Ryter A., Hofnung M. Antibodies against synthetic peptides and the topology of LamB, an outer membrane protein from Escherichia coli K12. Biochemistry. 28:1989;8234-8241.
    • (1989) Biochemistry , vol.28 , pp. 8234-8241
    • Molla, A.1    Charbit, A.2    Le Guern, A.3    Ryter, A.4    Hofnung, M.5
  • 41
    • 0033056654 scopus 로고    scopus 로고
    • Effect of loop deletions on the binding and transport of ferric enterobactin by FepA
    • Newton S.M., Igo J.D., Scott D.C., Klebba P.E. Effect of loop deletions on the binding and transport of ferric enterobactin by FepA. Mol. Microbiol. 32:1999;1153-1165.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1153-1165
    • Newton, S.M.1    Igo, J.D.2    Scott, D.C.3    Klebba, P.E.4
  • 42
    • 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., Klebba P.E., Michel V., Hofnung M., Charbit A. Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J. Bacteriol. 178:1996;3447-3456.
    • (1996) J. Bacteriol. , vol.178 , pp. 3447-3456
    • Newton, S.M.1    Klebba, P.E.2    Michel, V.3    Hofnung, M.4    Charbit, A.5
  • 43
    • 0017227534 scopus 로고
    • Outer membrane of Salmonella typhimurium. Transmembrane diffusion of some hydrophobic substances
    • Nikaido H. Outer membrane of Salmonella typhimurium. Transmembrane diffusion of some hydrophobic substances. Biochim. Biophys. Acta. 433:1976;118-132.
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 118-132
    • Nikaido, H.1
  • 44
    • 0018470992 scopus 로고
    • Permeability of the outer membrane of bacteria
    • Nikaido H. Permeability of the outer membrane of bacteria. Angew. Chem. Int. Ed. Engl. 18:1979;337-350.
    • (1979) Angew. Chem. Int. Ed. Engl. , vol.18 , pp. 337-350
    • Nikaido, H.1
  • 45
    • 0018587209 scopus 로고
    • The outer membrane of Gram-negative bacteria
    • Nikaido H., Nakae T. The outer membrane of Gram-negative bacteria. Adv. Microb. Physiol. 20:1979;163-250.
    • (1979) Adv. Microb. Physiol. , vol.20 , pp. 163-250
    • Nikaido, H.1    Nakae, T.2
  • 46
    • 0019824138 scopus 로고
    • Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli
    • Nikaido H., Rosenberg E.Y. Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J. Gen. Physiol. 77:1981;121-135.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 121-135
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 47
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins
    • Nikaido H., Rosenberg E.Y. Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins. J. Bacteriol. 153:1983;241-252.
    • (1983) J. Bacteriol. , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 48
    • 0020522392 scopus 로고
    • Porin channels in Escherichia coli: Studies with beta-lactams in intact cells
    • Nikaido H., Rosenberg E.Y., Foulds J. Porin channels in Escherichia coli: Studies with beta-lactams in intact cells. J. Bacteriol. 153:1983;232-240.
    • (1983) J. Bacteriol. , vol.153 , pp. 232-240
    • Nikaido, H.1    Rosenberg, E.Y.2    Foulds, J.3
  • 49
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1985;1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 50
    • 0036232212 scopus 로고    scopus 로고
    • Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (Maltoporin) channel of Escherichia coli. I. Effect on Ion
    • Orlik F., Andersen C., Benz R. Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (Maltoporin) channel of Escherichia coli. I. Effect on Ion. Transport. Biophys. J. 82:2002;2466-2475.
    • (2002) Transport. Biophys. J. , vol.82 , pp. 2466-2475
    • Orlik, F.1    Andersen, C.2    Benz, R.3
  • 51
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 52
    • 0015713398 scopus 로고
    • Isolation of the bacteriophage lambda receptor from Escherichia coli
    • Randall-Hazelbauer L., Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J. Bacteriol. 116:1973;1436-1446.
    • (1973) J. Bacteriol. , vol.116 , pp. 1436-1446
    • Randall-Hazelbauer, L.1    Schwartz, M.2
  • 53
    • 0025185218 scopus 로고
    • Export of altered forms of an Escherichia coli K-12 outer membrane protein (OmpA) can inhibit synthesis of unrelated outer membrane proteins
    • Ried G., MacIntyre S., Mutschler B., Henning U. Export of altered forms of an Escherichia coli K-12 outer membrane protein (OmpA) can inhibit synthesis of unrelated outer membrane proteins. J. Mol. Biol. 216:1990;39-47.
    • (1990) J. Mol. Biol. , vol.216 , pp. 39-47
    • Ried, G.1    MacIntyre, S.2    Mutschler, B.3    Henning, U.4
  • 54
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution
    • Schirmer T., Keller T.A., Wang Y.F., Rosenbusch J.P. Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution. [see comments] Science. 267:1995;512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 55
    • 0016709158 scopus 로고
    • Reversible interaction between coliphage lambda and its receptor protein
    • Schwartz M. Reversible interaction between coliphage lambda and its receptor protein. J. Mol. Biol. 99:1975;185-201.
    • (1975) J. Mol. Biol. , vol.99 , pp. 185-201
    • Schwartz, M.1
  • 56
    • 0017036139 scopus 로고
    • Further studies on the binding of maltose to the maltose-binding protein of Escherichia coli
    • Schwartz M., Kellermann O., Szmelcman S., Hazelbauer G.L. Further studies on the binding of maltose to the maltose-binding protein of Escherichia coli. Eur. J. Biochem. 71:1976;167-170.
    • (1976) Eur. J. Biochem. , vol.71 , pp. 167-170
    • Schwartz, M.1    Kellermann, O.2    Szmelcman, S.3    Hazelbauer, G.L.4
  • 57
    • 0017127269 scopus 로고
    • Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching
    • Szmelcman S., Schwartz M., Silhavy T.J., Boos W. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur. J. Biochem. 65:1976;13-19.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 13-19
    • Szmelcman, S.1    Schwartz, M.2    Silhavy, T.J.3    Boos, W.4
  • 59
    • 0021182815 scopus 로고
    • High-sensitivity detection of newly induced LamB protein on the Escherichia coli cell surface
    • Vos-Scheperkeuter G.H., Hofnung M., Witholt B. High-sensitivity detection of newly induced LamB protein on the Escherichia coli cell surface. J. Bacteriol. 159:1984;435-439.
    • (1984) J. Bacteriol. , vol.159 , pp. 435-439
    • Vos-Scheperkeuter, G.H.1    Hofnung, M.2    Witholt, B.3
  • 60
    • 0017254020 scopus 로고
    • Siderophore protection against colicins M, B, V, and Ia in Escherichia coli
    • Wayne R., Frick K., Neilands J.B. Siderophore protection against colicins M, B, V, and Ia in Escherichia coli. J. Bacteriol. 126:1976;7-12.
    • (1976) J. Bacteriol. , vol.126 , pp. 7-12
    • Wayne, R.1    Frick, K.2    Neilands, J.B.3
  • 61
    • 0016441805 scopus 로고
    • Evidence for common binding sites for ferrichrome compounds and bacteriophage phi 80 in the cell envelope of Escherichia coli
    • Wayne R., Neilands J.B. Evidence for common binding sites for ferrichrome compounds and bacteriophage phi 80 in the cell envelope of Escherichia coli. J. Bacteriol. 121:1975;497-503.
    • (1975) J. Bacteriol. , vol.121 , pp. 497-503
    • Wayne, R.1    Neilands, J.B.2
  • 62
    • 0025345316 scopus 로고
    • The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution
    • Weiss M.S., Wacker T., Weckesser J., Welte W., Schulz G.E. The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution. FEBS Lett. 267:1990;268-272.
    • (1990) FEBS Lett. , vol.267 , pp. 268-272
    • Weiss, M.S.1    Wacker, T.2    Weckesser, J.3    Welte, W.4    Schulz, G.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.