Activation of rhodopsin: new insights from structural and biochemical studies.
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K. Palczewski | K. Hofmann | O. Ernst | K P Hofmann | T Okada | K Palczewski | T. Okada | O P Ernst
[1] K. Palczewski,et al. Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor , 2002, Chembiochem : a European journal of chemical biology.
[2] T. Ngo,et al. Functionally Discrete Mimics of Light-activated Rhodopsin Identified through Expression of Soluble Cytoplasmic Domains* , 2000, The Journal of Biological Chemistry.
[3] H. Lother,et al. AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration , 2000, Nature.
[4] K. Fahmy,et al. Transducin-dependent protonation of glutamic acid 134 in rhodopsin. , 2000, Biochemistry.
[5] M. Engelhard,et al. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II. , 2000, Journal of molecular biology.
[6] P. Ormos,et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin , 2000, Nature.
[7] A. Abell,et al. Constitutive activation of G protein-coupled receptors as a result of selective substitution of a conserved leucine residue in transmembrane helix III. , 2000, Molecular endocrinology.
[8] M. Sheves,et al. The molecular origin of the inhibition of transducin activation in rhodopsin lacking the 9-methyl group of the retinal chromophore: a UV-Vis and FTIR spectroscopic study. , 2000, Biochemistry.
[9] K. Nakanishi,et al. Movement of retinal along the visual transduction path. , 2000, Science.
[10] K. Hofmann,et al. FTIR spectroscopy of complexes formed between metarhodopsin II and C‐terminal peptides from the G‐protein α‐ and γ‐subunits , 2000 .
[11] P. Henklein,et al. Mutation of the Fourth Cytoplasmic Loop of Rhodopsin Affects Binding of Transducin and Peptides Derived from the Carboxyl-terminal Sequences of Transducin α and γ Subunits* , 2000, The Journal of Biological Chemistry.
[12] W. Gärtner,et al. Signaling States of Rhodopsin RETINAL PROVIDES A SCAFFOLD FOR ACTIVATING PROTON TRANSFER SWITCHES* , 2000 .
[13] K. Rothschild,et al. Chapter 1 Structure and mechanism of vertebrate visual pigments , 2000 .
[14] K. Hofmann. Chapter 3 Late photoproducts and signaling states of bovine rhodopsin , 2000 .
[15] G. Schultz,et al. Activation of the rod G-protein Gt by the thrombin receptor (PAR1) expressed in Sf9 cells. , 1999, European journal of biochemistry.
[16] T. Schwartz,et al. Conversion of agonist site to metal-ion chelator site in the beta(2)-adrenergic receptor. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[17] H Luecke,et al. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. , 1999, Science.
[18] G. Kochendoerfer,et al. How color visual pigments are tuned. , 1999, Trends in biochemical sciences.
[19] S. S. Lee,et al. Folding and Assembly in Rhodopsin , 1999, The Journal of Biological Chemistry.
[20] Thomas Gudermann,et al. Structural basis of G protein-coupled receptor function , 1999, Molecular and Cellular Endocrinology.
[21] K. Hofmann,et al. Signal transfer from rhodopsin to the G-protein: evidence for a two-site sequential fit mechanism. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[22] E C Hulme,et al. The Functional Topography of Transmembrane Domain 3 of the M1 Muscarinic Acetylcholine Receptor, Revealed by Scanning Mutagenesis* , 1999, The Journal of Biological Chemistry.
[23] J Nathans,et al. Molecular genetics of human retinal disease. , 1999, Annual review of genetics.
[24] Y. Shichida,et al. Visual pigment: G-protein-coupled receptor for light signals , 1998, Cellular and Molecular Life Sciences CMLS.
[25] P. Hargrave,et al. Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[26] S. O. Smith,et al. Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6. , 1998, Biochemistry.
[27] T. Sakmar. Rhodopsin: a prototypical G protein-coupled receptor. , 1998, Progress in nucleic acid research and molecular biology.
[28] H. Khorana,et al. Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[29] C. Cowan,et al. A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. , 1997, Biophysical journal.
[30] J. Baldwin,et al. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. , 1997, Journal of molecular biology.
[31] Gebhard F. X. Schertler,et al. Arrangement of rhodopsin transmembrane α-helices , 1997, Nature.
[32] A. Scheer,et al. The activation process of the alpha1B-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[33] E A Merritt,et al. Raster3D: photorealistic molecular graphics. , 1997, Methods in enzymology.
[34] H. Khorana,et al. Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin , 1996, Science.
[35] D. Kliger,et al. Spectral and Kinetic Characterization of Visual Pigment Photointermediates , 1995 .
[36] J. Spudich. Protein-protein interaction converts a proton pump into a sensory receptor , 1994, Cell.
[37] K. Fahmy,et al. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. , 1994, The Journal of biological chemistry.
[38] K. Fahmy,et al. Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. , 1994, Biochemistry.
[39] M. Sheves,et al. Interactions of the beta-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins. , 1994, Biochemistry.
[40] K. Palczewski,et al. Control of rhodopsin multiple phosphorylation. , 1994, Biochemistry.
[41] K. Hideg,et al. Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. , 1993, Science.
[42] K. Hofmann,et al. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[43] D. Oprian,et al. Constitutive activation of opsin: influence of charge at position 134 and size at position 296. , 1993, Biochemistry.
[44] Gebhard F. X. Schertler,et al. Projection structure of rhodopsin , 1993, Nature.
[45] D. Oprian,et al. Identification of the Cl(-)-binding site in the human red and green color vision pigments. , 1993, Biochemistry.
[46] D. Oprian,et al. Constitutively active mutants of rhodopsin , 1992, Neuron.
[47] D. Oprian,et al. The ligand-binding domain of rhodopsin and other G protein-linked receptors , 1992, Journal of bioenergetics and biomembranes.
[48] P. Hargrave,et al. Rhodopsin and phototransduction: a model system for G protein‐linked receptors , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[49] M. Gutman,et al. The dynamic aspects of proton transfer processes , 1990 .
[50] R. Mathies,et al. Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: chromophore structure and energy storage in the primary photoproduct of vision. , 1989, Biochemistry.
[51] N. W. Downer,et al. Transient dichroism in photoreceptor membranes indicates that stable oligomers of rhodopsin do not form during excitation. , 1985, Biophysical journal.
[52] A. Cooper. Energy uptake in the first step of visual excitation , 1979, Nature.
[53] Carolyn A. Converse,et al. Energetics of primary processes in visula escitation: photocalorimetry of rhodopsin in rod outer segment membranes. , 1976, Biochemistry.
[54] S. Hecht,et al. ENERGY, QUANTA, AND VISION , 1942, The Journal of general physiology.