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0033005319
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Bacterial rhodopsins: Evolution of a mechanistic model for the ion pumps
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A historical review of bacteriorhodopsin research over the past 30 years
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Protein Sci
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Stoeckenius, W.1
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0025292355
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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
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Beckmann, E.5
Downing, K.H.6
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3
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0029903197
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Electron-crystallographic refinement of the structure of bacteriorhodopsin
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Grigorieff N, Ceska TA, Downing KH, Baldwin JM, Henderson R: Electron-crystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol 1996, 259:393-421.
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Grigorieff, N.1
Ceska, T.A.2
Downing, K.H.3
Baldwin, J.M.4
Henderson, R.5
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4
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0030768310
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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
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Kimura Y, Vassylyev DG, Miyazawa A, Kidera A, Matsushima M, Mitsuoka K, Murata K, Hirai T, Fujiyoshi Y: Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature 1997, 389:206-211.
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Nature
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Kimura, Y.1
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Mitsuoka, K.6
Murata, K.7
Hirai, T.8
Fujiyoshi, Y.9
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5
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0030864048
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X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
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Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM: X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 1997, 277:1676-1681.
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Science
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Pebay-Peyroula, E.1
Rummel, G.2
Rosenbusch, J.P.3
Landau, E.M.4
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6
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0032546920
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Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
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A model (PDB entry code 1brx) for the structure of bacteriorhodopsin was derived using X-ray diffraction data from three-dimensional crystals that diffract to a resolution of 2.3 Å. The crystals were obtained using exactly the same conditions employed in [10]. As in [5], the structure was solved by molecular replacement, using the coordinates derived from the earlier electron crystallographic work as a reference. Effort was made to account for the near-perfect twinning of the crystals in the refinement protocol used
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Luecke H, Richter HT, Lanyi JK: Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 1998, 280:1934-1937. A model (PDB entry code 1brx) for the structure of bacteriorhodopsin was derived using X-ray diffraction data from three-dimensional crystals that diffract to a resolution of 2.3 Å. The crystals were obtained using exactly the same conditions employed in [10]. As in [5], the structure was solved by molecular replacement, using the coordinates derived from the earlier electron crystallographic work as a reference. Effort was made to account for the near-perfect twinning of the crystals in the refinement protocol used.
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Science
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Luecke, H.1
Richter, H.T.2
Lanyi, J.K.3
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7
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0033605231
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The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
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The authors report an improved structure for bacteriorhodopsin (PDB entry code 2at9) obtained by electron crystallographic refinement of the model derived in [4]
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Mitsuoka K, Hirai T, Murata K, Miyazawa A, Kidera A, Kimura Y, Fujiyoshi Y: The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution. J Mol Biol 1999, 286:861-882. The authors report an improved structure for bacteriorhodopsin (PDB entry code 2at9) obtained by electron crystallographic refinement of the model derived in [4].
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J Mol Biol
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Mitsuoka, K.1
Hirai, T.2
Murata, K.3
Miyazawa, A.4
Kidera, A.5
Kimura, Y.6
Fujiyoshi, Y.7
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8
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0032578378
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Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
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A 2.9 Å resolution structure derived from X-ray crystallographic analysis of a monoclinic crystal form of bacteriorhodopsin is described
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Essen LO, Siegert R, Lehmannn WD, Oesterhelt D: Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proc Natl Acad Sci USA 1998, 95:11673-11678. A 2.9 Å resolution structure derived from X-ray crystallographic analysis of a monoclinic crystal form of bacteriorhodopsin is described.
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Proc Natl Acad Sci USA
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Essen, L.O.1
Siegert, R.2
Lehmannn, W.D.3
Oesterhelt, D.4
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9
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0032561127
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A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
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Takeda K, Sato H, Hino T, Kono M, Fukuda K, Sakurai J, Okada T, Kouyama T: A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J Mol Biol 1998, 283:463-474.
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Okada, T.7
Kouyama, T.8
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0029992660
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Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
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Landau, E.M.1
Rosenbusch, J.P.2
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11
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0027504943
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Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3 Å resolution
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Schertler GFX, Bartunik HD, Michel H, Oesterhelt D: Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3 Å resolution. J Mol Biol 1993, 234:156-164.
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Schertler, G.F.X.1
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Michel, H.3
Oesterhelt, D.4
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12
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0032502747
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Refolding of bacteriorhodopsin from expressed polypeptide fragments
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A detailed study of the association of different combinations of bacteriorhodopsin fragments that demonstrates that covalent connections in each of the three cytoplasmic and three extracellular surface loops of bacteriorhodopsin are dispensable for correct folding and chromophore formation
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Marti T: Refolding of bacteriorhodopsin from expressed polypeptide fragments. J Biol Chem 1998, 273:9312-9322. A detailed study of the association of different combinations of bacteriorhodopsin fragments that demonstrates that covalent connections in each of the three cytoplasmic and three extracellular surface loops of bacteriorhodopsin are dispensable for correct folding and chromophore formation.
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J Biol Chem
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Marti, T.1
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0040298977
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Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
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Müller DJ, Sass HJ, Müller SA, Büldt G, Engel A: Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J Mol Biol 1999, 285:1903-1909.
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Müller, D.J.1
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Büldt, G.4
Engel, A.5
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14
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0030808219
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Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
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Balashov SP, Imasheva ES, Ebrey TG, Chen N, Menick DR, Crouch RK: Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry 1997, 36:8671-8676.
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Balashov, S.P.1
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Ebrey, T.G.3
Chen, N.4
Menick, D.R.5
Crouch, R.K.6
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15
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0032562215
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Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
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Dioumaev AK, Richter HT, Brown LS, Tanio M, Tuzi S, Saito H, Kimura Y, Needleman R, Lanyi JK: Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry 1998, 37:2496-2506.
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Dioumaev, A.K.1
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Saito, H.6
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Needleman, R.8
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Mechanism of light-dependent proton translocation by bacteriorhodopsin
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0033573864
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The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH
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Balashov SP, Lu M, Imasheva ES, Govindjee R, Ebrey TG, Othersen B, Chen Y, Crouch RK, Menick DR: The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH. Biochemistry 1999, 38:2026-2039.
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Othersen, B.6
Chen, Y.7
Crouch, R.K.8
Menick, D.R.9
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19
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0030588770
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Conformational flexibility of arginine-82 as source for the heterogeneous and pH-dependent kinetics of the primary proton transfer step in the bacteriorhodopsin photocycle: An electrostatic model
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Scharnagl C, Fischer SF: Conformational flexibility of arginine-82 as source for the heterogeneous and pH-dependent kinetics of the primary proton transfer step in the bacteriorhodopsin photocycle: An electrostatic model. Chem Phys 1996, 212:231-246.
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0033514389
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Arginine activity in the proton-motive photocycle of bacteriorhodopsin: Solid-state NMR studies of the wild-type and D85N proteins
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Petkova AT, Hu JG, Bizounok M, Simpson M, Griffin RG, Herzfeld J: Arginine activity in the proton-motive photocycle of bacteriorhodopsin: Solid-state NMR studies of the wild-type and D85N proteins. Biochemistry 1999, 38:1562-1572.
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Biochemistry
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Petkova, A.T.1
Hu, J.G.2
Bizounok, M.3
Simpson, M.4
Griffin, R.G.5
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Molecular structure determination by electron microscopy of unstained crystalline specimens
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Protein crystals and their evil twins
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Yeates, T.O.1
Fam, B.C.2
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0032949908
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Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns
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Faruqi AR, Henderson R, Subramaniam S: Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns. Ultramicroscopy 1999, 75:235-250.
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Faruqi, A.R.1
Henderson, R.2
Subramaniam, S.3
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0032551761
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Detection of threonine structural changes upon formation of the M-intermediate of bacteriorhodopsin: Evidence for assignment to Thr-89
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Liu X, Lee MJ, Coleman M, Rath P, Nilsson A, Fischer WB, Bizounok M, Herzfeld J, Karstens WF, Raap J et al.: Detection of threonine structural changes upon formation of the M-intermediate of bacteriorhodopsin: Evidence for assignment to Thr-89. Biochim Biophys Acta 1998, 1365:363-372.
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0032474471
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Early and late M intermediates in the bacteriorhodopsin photocycle: A solid-state NMR study
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Hu JG, Sun BQ, Bizounok M, Hatcher ME, Lansing JC, Raap J, Verdegem PJ, Lugtenburg J, Griffin RG, Herzfeld J: Early and late M intermediates in the bacteriorhodopsin photocycle: A solid-state NMR study. Biochemistry 1998, 37:8088-8096.
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Herzfeld, J.10
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0033582945
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Protein conformational changes in the bacteriorhodopsin photocycle
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2, N and O) are well approximated by the other protein conformation, in which the Schiff base has access to the cytoplasmic side.
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Subramaniam, S.1
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Brown, L.7
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Henderson, R.9
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27
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0031021374
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General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
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Haupts U, Tittor J, Bamberg E, Oesterhelt D: General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model. Biochemistry 1997, 36:2-7.
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0032539982
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Local-access model for proton transfer in bacteriorhodopsin
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