메뉴 건너뛰기




Volumn 79, Issue 4, 2000, Pages 2066-2074

Selectivity in lipid binding to the bacterial outer membrane protein OmpF

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; PORIN;

EID: 0033798841     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76454-X     Document Type: Article
Times cited : (73)

References (12)
  • 1
    • 0032536195 scopus 로고    scopus 로고
    • Voltage-gating of Escherichia coli porin: A cysteine-scanning mutagenesis study of loop 3
    • Bainbridge, G., H. Mobasheri, G. A. Armstrong, E. J. A. Lea, and, J. H. Lakey. 1998. Voltage-gating of Escherichia coli porin: a cysteine-scanning mutagenesis study of loop 3. J. Mol. Biol. 275:171-176.
    • (1998) J. Mol. Biol. , vol.275 , pp. 171-176
    • Bainbridge, G.1    Mobasheri, H.2    Armstrong, G.A.3    Lea, E.J.A.4    Lakey, J.H.5
  • 2
    • 77957046824 scopus 로고
    • Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid bilayers
    • R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam
    • Ben-Shaul, A. 1995. Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid bilayers. In Handbook of Biological Physics, Vol. 1A, Structure and Dynamics of Membranes. R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam. 359-401.
    • (1995) Handbook of Biological Physics, Vol. 1A, Structure and Dynamics of Membranes , vol.1 A , pp. 359-401
    • Ben-Shaul, A.1
  • 3
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 4
    • 0027328751 scopus 로고
    • Bacterial porins: Lessons from three high-resolution structures
    • Cowan, S. W. 1993. Bacterial porins: lessons from three high-resolution structures. Gurr. Opin. Struct. Biol. 3:501-507.
    • (1993) Gurr. Opin. Struct. Biol. , vol.3 , pp. 501-507
    • Cowan, S.W.1
  • 6
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
    • Dumas, F., M. C. Lebrun, and J. F. Tocanne. 1999. Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions? FEBS Lett. 458:271-277.
    • (1999) FEBS Lett. , vol.458 , pp. 271-277
    • Dumas, F.1    Lebrun, M.C.2    Tocanne, J.F.3
  • 7
    • 0030823233 scopus 로고    scopus 로고
    • Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoylphosphatidylcholine lipid bilayers
    • Dumas, F., M. M. Sperotto, M. C. Lebrun, J. F. Tocanne, and O. G. Mouritsen. 1997. Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoylphosphatidylcholine lipid bilayers. Biophys. J. 73:1940-1953.
    • (1997) Biophys. J. , vol.73 , pp. 1940-1953
    • Dumas, F.1    Sperotto, M.M.2    Lebrun, M.C.3    Tocanne, J.F.4    Mouritsen, O.G.5
  • 8
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: The case of the calcium pump
    • Lee, A. G. 1998. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta. 1376:381-390.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 381-390
    • Lee, A.G.1
  • 9
    • 0021104115 scopus 로고
    • Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses
    • Lewis, B. A., and D. M. Engelman. 1983a. Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses. J. Mol. Biol. 166:203-210.
    • (1983) J. Mol. Biol. , vol.166 , pp. 203-210
    • Lewis, B.A.1    Engelman, D.M.2
  • 10
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis, B. A., and D. M. Engelman. 1983b. Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166:211-217.
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 11
    • 0019891873 scopus 로고
    • Fluorescence quenching in model membranes. 1. Characterization of quenching caused by a spin-labeled phospholipid
    • London, E., and G. W. Feigenson. 1981a. Fluorescence quenching in model membranes. 1. Characterization of quenching caused by a spin-labeled phospholipid. Biochemistry. 20:1932-1938.
    • (1981) Biochemistry , vol.20 , pp. 1932-1938
    • London, E.1    Feigenson, G.W.2
  • 12
    • 0032512417 scopus 로고    scopus 로고
    • Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: A possible mechanism of Golgi retention
    • Webb, R. J., J. M. East, R. P. Sharma, and A. G. Lee. 1998. Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: a possible mechanism of Golgi retention. Biochemistry. 37:673-679.
    • (1998) Biochemistry , vol.37 , pp. 673-679
    • Webb, R.J.1    East, J.M.2    Sharma, R.P.3    Lee, A.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.