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Volumn 128, Issue 1, 1999, Pages 119-130

Formation of helical protein assemblies of IgG and transducin on varied lipid tubules

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; IMMUNOGLOBULIN G; TRANSDUCIN;

EID: 0033388910     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1999.4151     Document Type: Article
Times cited : (20)

References (38)
  • 1
    • 0026779243 scopus 로고
    • Characterization of the aluminum and beryllium fluoride species which activate transducin
    • Antonny B., Chabre M. Characterization of the aluminum and beryllium fluoride species which activate transducin. J. Biol. Chem. 267:1992;6710-6718.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6710-6718
    • Antonny, B.1    Chabre, M.2
  • 2
    • 0029670614 scopus 로고    scopus 로고
    • Visualization of beta sheets and side-chain clusters in 2-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography
    • Avila-Sakar A. J., Chiu W. Visualization of beta sheets and side-chain clusters in 2-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys. J. 70:1996;57-68.
    • (1996) Biophys. J. , vol.70 , pp. 57-68
    • Avila-Sakar, A.J.1    Chiu, W.2
  • 3
    • 0022367326 scopus 로고
    • Fluoroaluminates activate transducin-GDP by mimicking the gamma-phosphate of GTP in its binding site
    • Bigay J., Deterre P., Pfister C., Chabre M. Fluoroaluminates activate transducin-GDP by mimicking the gamma-phosphate of GTP in its binding site. FEBS Lett. 191:1985;181-185.
    • (1985) FEBS Lett. , vol.191 , pp. 181-185
    • Bigay, J.1    Deterre, P.2    Pfister, C.3    Chabre, M.4
  • 4
    • 0020482336 scopus 로고
    • Minimal size phosphatidylcholine vesicles: Effects of radius of curvature on head group packing and conformation
    • Brouillette C. G., Segrest J. P., Ng T. C., Jones J. L. Minimal size phosphatidylcholine vesicles: Effects of radius of curvature on head group packing and conformation. Biochemistry. 21:1982;4569-4575.
    • (1982) Biochemistry , vol.21 , pp. 4569-4575
    • Brouillette, C.G.1    Segrest, J.P.2    Ng, T.C.3    Jones, J.L.4
  • 5
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey M., Feigenson G. W. Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry. 20:1981;1949-1961.
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 6
  • 7
    • 0032463742 scopus 로고    scopus 로고
    • Insights into Escherichia coli RNA polymerase structure from a combination of X-ray and electron crystallography
    • Darst S. A., Polyakov A., Richter C., Zhang G. Insights into Escherichia coli RNA polymerase structure from a combination of X-ray and electron crystallography. J. Struct. Biol. 124:1998;115-122.
    • (1998) J. Struct. Biol. , vol.124 , pp. 115-122
    • Darst, S.A.1    Polyakov, A.2    Richter, C.3    Zhang, G.4
  • 8
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs of structures with helial symmetry
    • DeRosier D. J., Moore P. B. Reconstruction of three-dimensional images from electron micrographs of structures with helial symmetry. J. Mol. Biol. 52:1970;355-369.
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • Derosier, D.J.1    Moore, P.B.2
  • 9
    • 0025046234 scopus 로고
    • Farnesylated gamma-subunit of photoreceptor G protein indispensable for GTP-binding
    • Fukada Y., Takao T., Ohguro H., Yoshizawa T., Akino T., Shimonishi Y. Farnesylated gamma-subunit of photoreceptor G protein indispensable for GTP-binding. Nature. 346:1990;658-660.
    • (1990) Nature , vol.346 , pp. 658-660
    • Fukada, Y.1    Takao, T.2    Ohguro, H.3    Yoshizawa, T.4    Akino, T.5    Shimonishi, Y.6
  • 10
    • 0013823053 scopus 로고
    • A new method of preparation of a self-perforated micro plastic grid and its application
    • Fukami A., Adachi K. A new method of preparation of a self-perforated micro plastic grid and its application. J. Electron Microsc. 14:1965;112-118.
    • (1965) J. Electron Microsc. , vol.14 , pp. 112-118
    • Fukami, A.1    Adachi, K.2
  • 11
    • 0021079937 scopus 로고
    • Characterization of transducin from bovine retinal rod outer segments. I. Separation and reconstitution of the subunits
    • Fung B. K. Characterization of transducin from bovine retinal rod outer segments. I. Separation and reconstitution of the subunits. J. Biol. Chem. 258:1983;10495-10502.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10495-10502
    • Fung, B.K.1
  • 12
    • 0000519923 scopus 로고
    • Flow of information in the light-triggered nucleotide cascade of vision
    • Fung B. K.-K., Hurley J. B., Stryer L. Flow of information in the light-triggered nucleotide cascade of vision. Proc. Natl. Acad. Sci. USA. 78:1981;152-156.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 152-156
    • Fung, B.K.-K.1    Hurley, J.B.2    Stryer, L.3
  • 13
    • 0029898061 scopus 로고    scopus 로고
    • A brief description of I.C.E.: The integrated crystallographic environment
    • Hardt S., Wang B., Schmid M. F. A brief description of I.C.E.: The integrated crystallographic environment. J. Struct. Biol. 116:1996;68-70.
    • (1996) J. Struct. Biol. , vol.116 , pp. 68-70
    • Hardt, S.1    Wang, B.2    Schmid, M.F.3
  • 14
    • 0031017896 scopus 로고    scopus 로고
    • Refined structure of an intact IgG2a monoclonal antibody
    • Harris L. J., Larson S. B., Hasel K. W., McPherson A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry. 36:1997;1581-1597.
    • (1997) Biochemistry , vol.36 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    McPherson, A.4
  • 15
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J., Schmid S. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature. 374:1995;190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.1    Schmid, S.2
  • 18
    • 0017902847 scopus 로고
    • Hydrodynamic analysis of egg phosphatidylcholine vesicles
    • Mason J. T., Huang C. Hydrodynamic analysis of egg phosphatidylcholine vesicles. Ann. N.Y. Acad. Sci. 308:1978;29-49.
    • (1978) Ann. N.Y. Acad. Sci. , vol.308 , pp. 29-49
    • Mason, J.T.1    Huang, C.2
  • 19
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin
    • Melia T. J., Cowan C. W., Angleson J. K., Wensel T. G. A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophys. J. 73:1997;3182-3191.
    • (1997) Biophys. J. , vol.73 , pp. 3182-3191
    • Melia, T.J.1    Cowan, C.W.2    Angleson, J.K.3    Wensel, T.G.4
  • 20
    • 0021233505 scopus 로고
    • Characterization of transducin from bovine retinal rod outer segments: Mechanism and effects of cholera toxin-catalyzed ADP-ribosylation
    • Navon S. E., Fung B. K. Characterization of transducin from bovine retinal rod outer segments: Mechanism and effects of cholera toxin-catalyzed ADP-ribosylation. J. Biol. Chem. 259:1984;6686-6693.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6686-6693
    • Navon, S.E.1    Fung, B.K.2
  • 21
    • 0028875725 scopus 로고
    • Three-dimensional structure of E. coli core RNA polymerase: Promoter binding and elongation conformations of the enzyme
    • Polyakov A., Severinova E., Darst S. A. Three-dimensional structure of E. coli core RNA polymerase: Promoter binding and elongation conformations of the enzyme. Cell. 83:1995;365-373.
    • (1995) Cell , vol.83 , pp. 365-373
    • Polyakov, A.1    Severinova, E.2    Darst, S.A.3
  • 23
    • 0343580439 scopus 로고    scopus 로고
    • Functionalized lipid tubules as tools for helical crystallization of proteins
    • Ringler P., Muller W., Ringsdorf H., Brisson A. Functionalized lipid tubules as tools for helical crystallization of proteins. Chem. Eur. J. 3:1997;620-625.
    • (1997) Chem. Eur. J. , vol.3 , pp. 620-625
    • Ringler, P.1    Muller, W.2    Ringsdorf, H.3    Brisson, A.4
  • 24
    • 0027554794 scopus 로고
    • SPECTRA: A system for processing electron images of crystals
    • Schmid M. F., Dargahi R., Tam M. W. SPECTRA: A system for processing electron images of crystals. Ultramicroscopy. 48:1993a;251-164.
    • (1993) Ultramicroscopy , vol.48 , pp. 251-164
    • Schmid, M.F.1    Dargahi, R.2    Tam, M.W.3
  • 25
    • 0027282605 scopus 로고
    • Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles
    • Schmid M. F., Robinson J. P., DasGupta B. R. Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles. Nature. 364:1993b;827-830.
    • (1993) Nature , vol.364 , pp. 827-830
    • Schmid, M.F.1    Robinson, J.P.2    Dasgupta, B.R.3
  • 26
    • 1642370200 scopus 로고
    • Lipid tubules: A paradigm for molecularly engineered structures
    • Schnur J. M. Lipid tubules: A paradigm for molecularly engineered structures. Science. 262:1993;1669-1676.
    • (1993) Science , vol.262 , pp. 1669-1676
    • Schnur, J.M.1
  • 27
    • 0022259825 scopus 로고
    • Photoreceptor GTP binding protein mediates fluoride activation of phosphodiesterase
    • Stein P. J., Halliday K. R., Rasenick M. M. Photoreceptor GTP binding protein mediates fluoride activation of phosphodiesterase. J. Biol. Chem. 260:1985;9081-9084.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9081-9084
    • Stein, P.J.1    Halliday, K.R.2    Rasenick, M.M.3
  • 28
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S. M., Hinshaw J. E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell. 93:1998;1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 29
    • 0032503947 scopus 로고    scopus 로고
    • Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes
    • Takei K., Haucke B., Slepnev V., Farsad K., Salazar M., Chen H., De Camilli P. Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell. 94:1998;131-141.
    • (1998) Cell , vol.94 , pp. 131-141
    • Takei, K.1    Haucke, B.2    Slepnev, V.3    Farsad, K.4    Salazar, M.5    Chen, H.6    De Camilli, P.7
  • 30
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K., McPherson P. S., Schmid S. L., De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature. 374:1995;186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 31
    • 0024701776 scopus 로고
    • On the use of holey grids in electron crystallography
    • Toyoshima C. On the use of holey grids in electron crystallography. Ultramicroscopy. 30:1989;439-444.
    • (1989) Ultramicroscopy , vol.30 , pp. 439-444
    • Toyoshima, C.1
  • 32
    • 0025202764 scopus 로고
    • Antibody organization on lipid films: Influence of pH and interchain disulfide reduction
    • Uzgiris E. E. Antibody organization on lipid films: Influence of pH and interchain disulfide reduction. Biochem. J. 272:1990;45-49.
    • (1990) Biochem. J. , vol.272 , pp. 45-49
    • Uzgiris, E.E.1
  • 33
    • 0020691229 scopus 로고
    • Two-dimensional crystallization technique for imaging macromolecules, with an application to antigen-antibody-complement complexes
    • Uzgiris E. E., Kornberg R. D. Two-dimensional crystallization technique for imaging macromolecules, with an application to antigen-antibody-complement complexes. Nature. 301:1983;125-129.
    • (1983) Nature , vol.301 , pp. 125-129
    • Uzgiris, E.E.1    Kornberg, R.D.2
  • 35
    • 0342712655 scopus 로고    scopus 로고
    • Heterotrimeric G proteins: Structure, regulation, and signaling mechanisms
    • A. Sitaramayya. Boston: Birkhauser
    • Wensel T. G. Heterotrimeric G proteins: Structure, regulation, and signaling mechanisms. Sitaramayya A. Introductory Signal Transduction. 1999;29-46 Birkhauser, Boston.
    • (1999) Introductory Signal Transduction , pp. 29-46
    • Wensel, T.G.1
  • 38
    • 0026445708 scopus 로고
    • N-myristoylation of the rod outer segment G protein, transducin, in cultured retinas
    • Yang Z., Wensel T. G. N-myristoylation of the rod outer segment G protein, transducin, in cultured retinas. J. Biol. Chem. 267:1992;23197-23201.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23197-23201
    • Yang, Z.1    Wensel, T.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.