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Volumn 187, Issue 24, 2005, Pages 8232-8236

The porinologist

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; ANTIBIOTIC AGENT; BACTERIAL PROTEIN; BACTERIUM LIPOPOLYSACCHARIDE; MALTODEXTRIN; MALTOSE; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; OUTER MEMBRANE PROTEIN F; PORIN;

EID: 28844497930     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.24.8232-8236.2005     Document Type: Short Survey
Times cited : (11)

References (24)
  • 1
    • 0015973774 scopus 로고
    • Protein composition of the outer membrane of salmonella typhimurium: Effect of lipopolysaccharide mutations
    • Ames, G, F., E, N. Spudich, and H. Nikaido. 1974. Protein composition of the outer membrane of Salmonella typhimurium: effect of lipopolysaccharide mutations J. Bacteriol. 117:406-416.
    • (1974) J. Bacteriol. , vol.117 , pp. 406-416
    • Ames, G.F.1    Spudich, E.N.2    Nikaido, H.3
  • 2
    • 0017648838 scopus 로고
    • Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein
    • Bavoil, P., H. Nikaido, and K, von Meyenburg. 1977. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol. Gen. Genet. 158:23-33.
    • (1977) Mol. Gen. Genet. , vol.158 , pp. 23-33
    • Bavoil, P.1    Nikaido, H.2    Von Meyenburg, K.3
  • 4
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A. L., H. A. Shuman, and H. Nikaido. 1992. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. USA 89:2360-2364.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 5
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 a resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber, and H. Michel. 1984. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180:385-398.
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 6
    • 9044236111 scopus 로고
    • Formation of protoplasts in mutant strains of Salmonella induced by galactose
    • Fukasawa, T., and H. Nikaido. 1959. Formation of protoplasts in mutant strains of Salmonella induced by galactose. Nature 183:1131-1132.
    • (1959) Nature , vol.183 , pp. 1131-1132
    • Fukasawa, T.1    Nikaido, H.2
  • 7
    • 0018895224 scopus 로고
    • Asymmetric localization of lipopoly-saccharides on the outer membrane of Salmonella typhimurium
    • Funahara, Y., and H. Nikaido. 1980. Asymmetric localization of lipopoly-saccharides on the outer membrane of Salmonella typhimurium. J. Bacteriol. 141:1463-1465.
    • (1980) J. Bacteriol. , vol.141 , pp. 1463-1465
    • Funahara, Y.1    Nikaido, H.2
  • 8
    • 0030764656 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein
    • Hall, J. A., K. Gehring, and H. Nikaido. 1997. Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein. J. Biol. Chem. 272:17605-17609.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17605-17609
    • Hall, J.A.1    Gehring, K.2    Nikaido, H.3
  • 9
    • 0030757501 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling
    • Hall, J. A., T. E. Thorgeirsson, J. Liu, Y. K. Shin, and H. Nikaido. 1997. Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling. J. Biol. Chem. 272:17610-17614.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17610-17614
    • Hall, J.A.1    Thorgeirsson, T.E.2    Liu, J.3    Shin, Y.K.4    Nikaido, H.5
  • 10
    • 0017188213 scopus 로고
    • Outer membrane of Salmonella typhimurium: Accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium
    • Kamio, Y., and H. Nikaido. 1976. Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium. Biochemistry 15:2561-2570.
    • (1976) Biochemistry , vol.15 , pp. 2561-2570
    • Kamio, Y.1    Nikaido, H.2
  • 12
    • 0028067837 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Resistance to tetracycline, chloramphenicol, and norfloxacin
    • Li, X. Z., D. M. Livermore, and H. Nikaido. 1994. Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: resistance to tetracycline, chloramphenicol, and norfloxacin. Antimicrob. Agents Chemother. 38:1732-1741.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1732-1741
    • Li, X.Z.1    Livermore, D.M.2    Nikaido, H.3
  • 13
    • 0028050605 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Active efflux as a contributing factor to beta-lactam resistance
    • Li, X. Z., D. Ma, D. M. Livermore, and H. Nikaido. 1994. Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: active efflux as a contributing factor to beta-lactam resistance. Antimicrob. Agents Chemother. 38:1742-1752.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1742-1752
    • Li, X.Z.1    Ma, D.2    Livermore, D.M.3    Nikaido, H.4
  • 14
    • 0029862802 scopus 로고    scopus 로고
    • Mycolic acid structure determines the fluidity of the mycobacterial cell wall
    • Liu, J., C. E. Barry III, G. S. Besra, and H. Nikaido. 1996. Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J. Biol. Chem. 271:29545-29551.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29545-29551
    • Liu, J.1    Barry III, C.E.2    Besra, G.S.3    Nikaido, H.4
  • 15
    • 0028820791 scopus 로고
    • Fluidity of the lipid domain of cell wall from Mycobacterium chelonae
    • Liu, J., E. Y. Rosenberg, and H. Nikaido. 1995. Fluidity of the lipid domain of cell wall from Mycobacterium chelonae. Proc. Natl. Acad. Sci. USA 92:11254-11258.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11254-11258
    • Liu, J.1    Rosenberg, E.Y.2    Nikaido, H.3
  • 16
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli
    • Luckey, M., and H. Nikaido. 1980. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc. Natl. Acad. Sci. USA 77:167-171.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 167-171
    • Luckey, M.1    Nikaido, H.2
  • 17
    • 0032953031 scopus 로고    scopus 로고
    • Microdermatology: Cell surface in the interaction of microbes with the external world
    • Nikaido, H. 1999. Microdermatology: cell surface in the interaction of microbes with the external world. J. Bacteriol. 181:4-8.
    • (1999) J. Bacteriol. , vol.181 , pp. 4-8
    • Nikaido, H.1
  • 18
    • 0027222842 scopus 로고
    • Physical organization of lipids in the cell wall of Mycobacterium chelonae
    • Nikaido, H., S. H. Kim, and E. Y. Rosenberg. 1993. Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol. Microbiol. 8:1025-1030.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1025-1030
    • Nikaido, H.1    Kim, S.H.2    Rosenberg, E.Y.3
  • 19
    • 0019824138 scopus 로고
    • Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli
    • Nikaido, H., and E. Y. Rosenberg. 1981. Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J. Gen. Physiol. 77:121-135.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 121-135
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 20
    • 0017687155 scopus 로고
    • Outer membrane of Salmonella XIV. Reduced transmembrane diffusion rates in porin-deficient mutants
    • Nikaido, H., S. A. Song, L. Shaltiel, and M. Nurminen. 1976. Outer membrane of Salmonella XIV. Reduced transmembrane diffusion rates in porin-deficient mutants. Biochem. Biophys. Res. Commun. 76:324-330.
    • (1976) Biochem. Biophys. Res. Commun. , vol.76 , pp. 324-330
    • Nikaido, H.1    Song, S.A.2    Shaltiel, L.3    Nurminen, M.4
  • 21
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and M. Vaara. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 22
    • 0023867105 scopus 로고
    • Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane
    • Sen, K., J. Hellman, and H. Nikaido. 1988. Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane. J. Biol. Chem. 263:1182-1187.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1182-1187
    • Sen, K.1    Hellman, J.2    Nikaido, H.3
  • 23
    • 0027064590 scopus 로고
    • Porins in the cell wall of mycobacteria
    • Trias, J, V. Jarlier, and R. Benz. 1992. Porins in the cell wall of mycobacteria. Science 258:1479-1481.
    • (1992) Science , vol.258 , pp. 1479-1481
    • Trias, J.1    Jarlier, V.2    Benz, R.3
  • 24
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • Yu, E. W., G. McDermott, H. I. Zgurskaya, H. Nikaido, and D. E. Koshland, Jr. 2003. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300:976-980.
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3    Nikaido, H.4    Koshland Jr., D.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.