| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0091-679X(07)84016-7 |
| P698 | PubMed publication ID | 17964941 |
| P2093 | author name string | George J Turner | |
| P2860 | cites work | Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium | Q24536703 |
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| Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution | Q27619516 | ||
| Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution | Q27619932 | ||
| Crystal structure of rhodopsin: A G protein-coupled receptor | Q27625972 | ||
| Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin | Q27626628 | ||
| Crystal structure of the D85S mutant of bacteriorhodopsin: model of an O-like photocycle intermediate | Q27635544 | ||
| Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle | Q27639574 | ||
| Mechanism of Proton Transport in Bacteriorhodopsin from Crystallographic Structures of the K, L, M1, M2, and M2′ Intermediates of the Photocycle | Q27640967 | ||
| Side-chain contributions to membrane protein structure and stability | Q27642725 | ||
| X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases | Q27742848 | ||
| Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation | Q37684251 | ||
| Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base | Q37684380 | ||
| pH-dependent processes in proteins. | Q39829724 | ||
| Forces and factors that contribute to the structural stability of membrane proteins | Q40594250 | ||
| Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. | Q40871637 | ||
| The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase | Q40918578 | ||
| Structural and genetic analysis of the folding and function of T4 lysozyme | Q40949115 | ||
| Sequence determinants of folding and stability for the P22 Arc repressor dimer. | Q40949119 | ||
| Modeling of G-protein-coupled receptors: application to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors | Q41086120 | ||
| An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors | Q41633574 | ||
| The third extracellular loop of the beta2-adrenergic receptor can modulate receptor/G protein affinity. | Q42451958 | ||
| Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: high-level expression in Escherichia coli | Q43017421 | ||
| Effects of Asp-96----Asn, Asp-85----Asn, and Arg-82----Gln single-site substitutions on the photocycle of bacteriorhodopsin | Q43795758 | ||
| Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the reprotonation mechanism | Q44060658 | ||
| Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base | Q44205486 | ||
| Synergistic contributions of the functional groups of epinephrine to its affinity and efficacy at the beta2 adrenergic receptor. | Q44854931 | ||
| Thermodynamics and energy coupling in the bacteriorhodopsin photocycle | Q45224917 | ||
| Bacteriorhodopsin D85N: three spectroscopic species in equilibrium | Q46051251 | ||
| Local-access model for proton transfer in bacteriorhodopsin | Q46285854 | ||
| A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin | Q46553431 | ||
| Identification of an agonist-induced conformational change occurring adjacent to the ligand-binding pocket of the M(3) muscarinic acetylcholine receptor | Q46644237 | ||
| An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces | Q46698156 | ||
| Agonist binding: a multistep process | Q47717572 | ||
| Heterologous gene expression in a membrane-protein-specific system | Q47915304 | ||
| Protein conformational changes during the bacteriorhodopsin photocycle. A Fourier transform infrared/resonance Raman study of the alkaline form of the mutant Asp-85-->Asn. | Q50755275 | ||
| Genetic transfer of the pigment bacteriorhodopsin into the eukaryoteSchizosaccharomyces pombe | Q57080276 | ||
| Spectroscopic Characterization of Bacteriorhodopsin's L-intermediate in 3D Crystals Cooled to 170 K¶ | Q58024032 | ||
| Chloroethylclonidine and 2-Aminoethyl Methanethiosulfonate Recognize Two Different Conformations of the Human α2A-Adrenergic Receptor | Q63431693 | ||
| Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin | Q68336802 | ||
| Substitution of membrane-embedded aspartic acids in bacteriorhodopsin causes specific changes in different steps of the photochemical cycle | Q69378465 | ||
| Probing structural and physical basis of protein energetics linked to protons and salt | Q70828930 | ||
| Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin | Q72819636 | ||
| Agonist-specific receptor conformations | Q74029094 | ||
| High-throughput screening of bacteriorhodopsin mutants in whole cell pastes | Q74420065 | ||
| Protein conformational changes in the bacteriorhodopsin photocycle | Q74599323 | ||
| Surface of bacteriorhodopsin revealed by high-resolution electron crystallography | Q27743232 | ||
| Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane | Q28241677 | ||
| Rapid evolution of a protein in vitro by DNA shuffling | Q28245873 | ||
| Membrane protein folding and stability: physical principles | Q29620789 | ||
| The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction | Q30312661 | ||
| Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin | Q30333704 | ||
| The progress of membrane protein structure determination | Q30342003 | ||
| Lysozyme: a paradigmatic molecule for the investigation of protein structure, function and misfolding. | Q30350768 | ||
| Role of aspartate-96 in proton translocation by bacteriorhodopsin. | Q30369152 | ||
| A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition | Q30423878 | ||
| Myoglobin: the hydrogen atom of biology and a paradigm of complexity | Q31149692 | ||
| Aspartic acid substitutions affect proton translocation by bacteriorhodopsin | Q33580073 | ||
| Interconversions of the M, N, and O intermediates in the bacteriorhodopsin photocycle. | Q33908133 | ||
| Reconciling crystallography and mutagenesis: a synthetic approach to the creation of a comprehensive model for proton pumping by bacteriorhodopsin | Q34030941 | ||
| Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycle | Q34087597 | ||
| Acetylcholine receptor channel structure probed in cysteine-substitution mutants. | Q34250941 | ||
| High-frequency spontaneous mutation in the bacterio-opsin gene in Halobacterium halobium is mediated by transposable elements | Q34254390 | ||
| Resolving pathways of functional coupling within protein assemblies by site-specific structural perturbation | Q34258006 | ||
| Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation | Q34337233 | ||
| Asymmetric cooperativity in a symmetric tetramer: human hemoglobin | Q34486165 | ||
| Inactivating mutations of G protein-coupled receptors and diseases: structure-function insights and therapeutic implications. | Q34514122 | ||
| Target validation of G-protein coupled receptors | Q34525952 | ||
| Structural basis of perturbed pKa values of catalytic groups in enzyme active sites | Q34670783 | ||
| Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N. | Q34722809 | ||
| Plasmid transformation of Escherichia coli and other bacteria | Q34980695 | ||
| Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: thymidylate synthase mutagenesis, function, and structure | Q35043987 | ||
| The present view of the mechanism of protein folding | Q35141764 | ||
| Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers | Q35531134 | ||
| Mutant G-protein-coupled receptors as a cause of human diseases | Q35958795 | ||
| In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy | Q36354305 | ||
| The bacteriorhodopsin gene | Q36377664 | ||
| Comparing function and structure between entire proteomes | Q36640722 | ||
| A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin | Q36764695 | ||
| Reversible steps in the bacteriorhodopsin photocycle | Q36965326 | ||
| P921 | main subject | membrane protein | Q423042 |
| P304 | page(s) | 479-515 | |
| P577 | publication date | 2008-01-01 | |
| P1433 | published in | Methods in Cell Biology | Q2638096 |
| P1476 | title | Mutagenic analysis of membrane protein functional mechanisms: bacteriorhodopsin as a model example | |
| P478 | volume | 84 |
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