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Volumn 74, Issue 3, 1998, Pages 1409-1420

Electron cryomicroscopy of bacteriorhodopsin vesicles: Mechanism of vesicle formation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; HALOLIPID; OCTYLTHIOGLUCOSIDE; UNCLASSIFIED DRUG;

EID: 0031932860     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77853-1     Document Type: Article
Times cited : (46)

References (51)
  • 2
    • 0028113702 scopus 로고
    • Bacteriorhodopsin: A nonlinear proton pump
    • Birge, R. R. 1994. Bacteriorhodopsin: a nonlinear proton pump. Nature. 371:659-660.
    • (1994) Nature , vol.371 , pp. 659-660
    • Birge, R.R.1
  • 4
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D. L. D., and A. Klug. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27:1-24.
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 6
    • 0030272726 scopus 로고    scopus 로고
    • Method for controlled formation of vitrified films for cryo-electron microscopy
    • Denkov, N. D., H. Yoshimura, and K. Nagayama. 1996a. Method for controlled formation of vitrified films for cryo-electron microscopy. Ultramicroscopy. 65:147-158.
    • (1996) Ultramicroscopy , vol.65 , pp. 147-158
    • Denkov, N.D.1    Yoshimura, H.2    Nagayama, K.3
  • 9
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. B. Jackson, editor. CRC Press, Boca Raton, FL
    • Ebrey, T. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membrane Receptors and Channels. M. B. Jackson, editor. CRC Press, Boca Raton, FL. 353-387.
    • (1993) Thermodynamics of Membrane Receptors and Channels , pp. 353-387
    • Ebrey, T.1
  • 10
    • 11944258697 scopus 로고
    • Entropy-driven tension and bending elasticity in condensed-fluid membranes
    • Evans, E., and W. Rawicz. 1990. Entropy-driven tension and bending elasticity in condensed-fluid membranes. Phys. Rev. Lett. 64: 2094-2097.
    • (1990) Phys. Rev. Lett. , vol.64 , pp. 2094-2097
    • Evans, E.1    Rawicz, W.2
  • 11
    • 0025260818 scopus 로고
    • Effect of partial delipidation of purple membrane on the photodynamics of bacteriorhodopsin
    • Fukuda, K., A. Ikegami, A. Nasuda-Kouyama, and T. Kouyama. 1990. Effect of partial delipidation of purple membrane on the photodynamics of bacteriorhodopsin. Biochemistry. 29:1997-2002.
    • (1990) Biochemistry , vol.29 , pp. 1997-2002
    • Fukuda, K.1    Ikegami, A.2    Nasuda-Kouyama, A.3    Kouyama, T.4
  • 12
  • 13
    • 21844451717 scopus 로고
    • Multiple modes of subunit association in the structures of simple spherical viruses
    • Harrison, S. C. 1984. Multiple modes of subunit association in the structures of simple spherical viruses. Trends Biochem. Sci. 9:345-351.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 345-351
    • Harrison, S.C.1
  • 14
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: Theory and possible experiments
    • Helfrich, W. 1973. Elastic properties of lipid bilayers: theory and possible experiments. Z. Naturforsch. C. 28:693-703.
    • (1973) Z. Naturforsch. C. , vol.28 , pp. 693-703
    • Helfrich, W.1
  • 15
    • 0016637383 scopus 로고
    • The structure of the purple membrane from Halobacterium halobium: Analysis of the x-ray diffraction pattern
    • Henderson, R. 1975. The structure of the purple membrane from Halobacterium halobium: analysis of the x-ray diffraction pattern. J. Mol. Biol. 93:123-138.
    • (1975) J. Mol. Biol. , vol.93 , pp. 123-138
    • Henderson, R.1
  • 16
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 17
    • 0018187260 scopus 로고
    • Specific labelling of the protein and lipid on the extracellular surface of purple membrane
    • Henderson, R., J. S. Jubb, and S. Whytock. 1978. Specific labelling of the protein and lipid on the extracellular surface of purple membrane. J. Mol. Biol. 123:259-274.
    • (1978) J. Mol. Biol. , vol.123 , pp. 259-274
    • Henderson, R.1    Jubb, J.S.2    Whytock, S.3
  • 18
    • 0019325326 scopus 로고
    • Crystallization of purple membrane in three dimensions
    • Henderson, R., and D. Shotton. 1980. Crystallization of purple membrane in three dimensions. J. Mol. Biol. 139:99-109.
    • (1980) J. Mol. Biol. , vol.139 , pp. 99-109
    • Henderson, R.1    Shotton, D.2
  • 19
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R., and P. N. T. Unwin. 1975. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 20
    • 0018654294 scopus 로고
    • The formation of virus crystalline and paracrystalline arrays for electron microscopy and image analysis
    • Horne, R. W. 1979. The formation of virus crystalline and paracrystalline arrays for electron microscopy and image analysis. Adv. Virus Res. 24:173-221.
    • (1979) Adv. Virus Res. , vol.24 , pp. 173-221
    • Horne, R.W.1
  • 21
    • 0016207970 scopus 로고
    • A negative staining carbon film technique for studying viruses in the electron microscope. I. Preparation procedures for examining icosahedral and filamentous viruses
    • Horne, R. W., and I. Pasquali-Ronchetti. 1974. A negative staining carbon film technique for studying viruses in the electron microscope. I. Preparation procedures for examining icosahedral and filamentous viruses. J. Ultrastruct. Res. 47:361-383.
    • (1974) J. Ultrastruct. Res. , vol.47 , pp. 361-383
    • Horne, R.W.1    Pasquali-Ronchetti, I.2
  • 22
    • 0017750496 scopus 로고
    • Refinement of the fluid-mosaic model of membrane structure
    • Israelachvili, J. N. 1977. Refinement of the fluid-mosaic model of membrane structure. Biochim. Biophys. Acta. 469:221-225.
    • (1977) Biochim. Biophys. Acta. , vol.469 , pp. 221-225
    • Israelachvili, J.N.1
  • 25
    • 21244499919 scopus 로고
    • Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
    • Kates, M., S. C. Kushwaha, and G. D. Sprott. 1982. Lipids of purple membrane from extreme halophiles and of methanogenic bacteria. Methods Enzymol. 88:98-111.
    • (1982) Methods Enzymol. , vol.88 , pp. 98-111
    • Kates, M.1    Kushwaha, S.C.2    Sprott, G.D.3
  • 26
    • 0027161989 scopus 로고
    • On the revised structure of the major phospholipid of Halobacterium salinarium
    • Kates, M., N. Moldoveanu, and L. C. Stewart. 1993. On the revised structure of the major phospholipid of Halobacterium salinarium. Biochim. Biophys. Acta. 1169:46-53.
    • (1993) Biochim. Biophys. Acta. , vol.1169 , pp. 46-53
    • Kates, M.1    Moldoveanu, N.2    Stewart, L.C.3
  • 27
    • 0027354448 scopus 로고
    • Storage and release of neurotransmitters
    • Kelly, R. B. 1993. Storage and release of neurotransmitters. Cell Neuron. 72:43-53.
    • (1993) Cell Neuron. , vol.72 , pp. 43-53
    • Kelly, R.B.1
  • 28
    • 0024278712 scopus 로고
    • Bacteriorhodopsin, a membrane protein that uses light to translocate protons
    • Khorana, H. G. 1988. Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263:7439-7442.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7439-7442
    • Khorana, H.G.1
  • 30
    • 0001542995 scopus 로고
    • The structure of small viruses
    • Klug, A., and D. L. D. Caspar. 1960. The structure of small viruses. Adv. Virus Res. 7:225-325.
    • (1960) Adv. Virus Res. , vol.7 , pp. 225-325
    • Klug, A.1    Caspar, D.L.D.2
  • 31
    • 0028763756 scopus 로고
    • Polyhedral assembly of a membrane protein in its three-dimensional crystal
    • Kouyama, T., M. Yamamoto, N. Kamiya, H. Iwasaki, T. Ueki, and I. Sakurai. 1994. Polyhedral assembly of a membrane protein in its three-dimensional crystal. J. Mol. Biol. 236:990-994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 990-994
    • Kouyama, T.1    Yamamoto, M.2    Kamiya, N.3    Iwasaki, H.4    Ueki, T.5    Sakurai, I.6
  • 32
    • 0028407552 scopus 로고
    • Theory of curved interfaces and membranes: Mechanical and thermodynamical approaches
    • Kralchevsky, P. A., J. C. Eriksson, and S. Ljunggren. 1994. Theory of curved interfaces and membranes: mechanical and thermodynamical approaches. Adv. Colloid Interface Sci. 48:19-59.
    • (1994) Adv. Colloid Interface Sci. , vol.48 , pp. 19-59
    • Kralchevsky, P.A.1    Eriksson, J.C.2    Ljunggren, S.3
  • 33
    • 0026908304 scopus 로고
    • Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins
    • Kreis, T. E. 1992. Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. Curr. Opin. Cell Biol. 4:609-615.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 609-615
    • Kreis, T.E.1
  • 34
    • 0024117785 scopus 로고
    • Three-dimensional crystallisation of membrane proteins
    • Kühlbrandt, W. 1988. Three-dimensional crystallisation of membrane proteins. Q. Rev. Biophys. 21:429-477.
    • (1988) Q. Rev. Biophys. , vol.21 , pp. 429-477
    • Kühlbrandt, W.1
  • 36
    • 0000664301 scopus 로고
    • Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals
    • Michel, H. 1982. Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals. EMBO J. 1:1267-1271.
    • (1982) EMBO J. , vol.1 , pp. 1267-1271
    • Michel, H.1
  • 37
    • 0000095071 scopus 로고
    • Three-dimensional crystals of membrane proteins: Bacteriorhodopsin
    • Michel, H., and D. Oesterhelt. 1980. Three-dimensional crystals of membrane proteins: bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 77: 1283-1285.
    • (1980) Proc. Natl. Acad. Sci. USA. , vol.77 , pp. 1283-1285
    • Michel, H.1    Oesterhelt, D.2
  • 40
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fragmentation into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fragmentation into red and purple membrane. Methods Enzymol. 31:667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 41
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orci, L., D. J. Palmer, M. Amherdt, and J. A. Rothman. 1993. Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature. 364:732-734.
    • (1993) Nature. , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.A.4
  • 43
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane: Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek, M., and M. P. Heyn. 1979. Binding of all-trans-retinal to the purple membrane: evidence for cooperativity and determination of the extinction coefficient. Biochemistry. 18:4977-4983.
    • (1979) Biochemistry. , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 46
    • 0027504943 scopus 로고
    • Orthorombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution
    • Schertler, G. F. X., H. D. Bartunik, H. Michel, and D. Oesterhelt. 1993. Orthorombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution. J. Mol. Biol. 234:156-164.
    • (1993) J. Mol. Biol. , vol.234 , pp. 156-164
    • Schertler, G.F.X.1    Bartunik, H.D.2    Michel, H.3    Oesterhelt, D.4
  • 48
    • 0002537845 scopus 로고
    • Bacteriorhodopsin: A molecular photooscillator?
    • Tributsch, H., and R. A. Bogomolni. 1994. Bacteriorhodopsin: a molecular photooscillator? Chem. Phys. Lett. 227:74-78.
    • (1994) Chem. Phys. Lett. , vol.227 , pp. 74-78
    • Tributsch, H.1    Bogomolni, R.A.2
  • 50
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin, P. N. T., and R. Henderson. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 51
    • 0018142627 scopus 로고
    • Properties of the two sides of the purple membrane correlated
    • Zingsheim, H. P., D.-Ch. Neugebauer, and R. Henderson. 1978. Properties of the two sides of the purple membrane correlated. J. Mol. Biol. 123:275-278.
    • (1978) J. Mol. Biol. , vol.123 , pp. 275-278
    • Zingsheim, H.P.1    Neugebauer, D.-Ch.2    Henderson, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.