Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

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BRET analysis of GPCR oligomerization: newer does not mean better

Bouvier, M., Heveker, N., Jockers, R., Marullo, S., & Milligan, G. (2006) · Nature Methods · doi:10.1038/nmeth0107-3 · Cited by 128

Role of THR-252 in Cytochrome P450CAM: A Study with Unnatural Amino Acid Mutagenesis

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The use of 5′-pbospho-2 deoxyribocytidylylriboadenosine as a facile route to chemical aminoacylation of tRNA

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An In Vivo Covalent TMP-Tag Based on Proximity-Induced Reactivity

Gallagher, S. S., Sable, J. E., Sheetz, M. P., & Cornish, V. W. (2009) · ACS Chemical Biology · doi:10.1021/cb900062k · Cited by 126

Fluorescence Correlation Spectroscopy Analysis of Serotonin, Adrenergic, Muscarinic, and Dopamine Receptor Dimerization: The Oligomer Number Puzzle

Herrick‐Davis, K., Grinde, E., Cowan, A. E., & Mazurkiewicz, J. E. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.087072 · Cited by 125

Imaging G protein–coupled receptors while quantifying their ligand-binding free-energy landscape

Alsteens, D., Pfreundschuh, M., Zhang, C., Spoerri, P. M., Coughlin, S. R., Kobilka, B. K., & Müller, D. J. (2015) · Nature Methods · doi:10.1038/nmeth.3479 · Cited by 124

Single Molecule Analysis of Functionally Asymmetric G Protein-coupled Receptor (GPCR) Oligomers Reveals Diverse Spatial and Structural Assemblies

Jonas, K., Fanelli, F., Huhtaniemi, I. T., & Hanyaloglu, A. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.622498 · Cited by 124

Identification and sequence of a binding site peptide of the .beta.2-adrenergic receptor

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Construction of a light-activated protein by unnatural amino acid mutagenesis

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NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution 19 F NMR

Klein‐Seetharaman, J., Getmanova, E. V., Loewen, M. C., Reeves, P. J., & Khorana, H. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13744 · Cited by 123

Quantitative analysis of the formation and diffusion of A 1 -adenosine receptor-antagonist complexes in single living cells

Briddon, S. J., Middleton, R. J., Cordeaux, Y., Flavin, F. M., Weinstein, J. A., George, M. W., Kellam, B., & Hill, S. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400420101 · Cited by 122

Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin

Resek, J. F., Farahbakhsh, Z. T., Hubbell, W. L., & Khorana, H. G. (1993) · Biochemistry · doi:10.1021/bi00096a012 · Cited by 119

Genetically Encoding Photoswitchable Click Amino Acids in Escherichia coli and Mammalian Cells

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Microscopy beyond the diffraction limit using actively controlled single molecules

Moerner, W. E. (2012) · Journal of Microscopy · doi:10.1111/j.1365-2818.2012.03600.x · Cited by 118

Polyspecific pyrrolysyl-tRNA synthetases from directed evolution

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Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking

Kallal, L. A., & Benovic, J. (2000) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01477-2 · Cited by 117

Luminescent Lanthanide Cryptates: from the Bench to the Bedside

Zwier, J. M., Bazin, H., Lamarque, L., & Mathis, G. (2014) · Inorganic Chemistry · doi:10.1021/ic402234k · Cited by 115

Adaptation of an Orthogonal Archaeal Leucyl-tRNA and Synthetase Pair for Four-base, Amber, and Opal Suppression

Anderson, J. C., & Schultz, P. G. (2003) · Biochemistry · doi:10.1021/bi034550w · Cited by 114

SPIN LABELED CYSTEINES AS SENSORS FOR PROTEIN‐LIPID INTERACTION AND CONFORMATION IN RHODOPSIN

Farahbakhsh, Z. T., Altenbach, C., & Hubbell, W. L. (1992) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1992.tb09725.x · Cited by 113

Rapid Incorporation of Functional Rhodopsin into Nanoscale Apolipoprotein Bound Bilayer (NABB) Particles

Banerjee, S., Huber, T., & Sakmar, T. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.066 · Cited by 113

Conformational states of the full-length glucagon receptor

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Mapping the Ligand-Binding Site on a G Protein-Coupled Receptor (GPCR) Using Genetically Encoded Photocrosslinkers

Grunbeck, A., Huber, T., Sachdev, P., & Sakmar, T. P. (2011) · Biochemistry · doi:10.1021/bi200214r · Cited by 112

Dynamics of β2-Adrenergic Receptor−Ligand Complexes on Living Cells

Hegener, O., Prenner, L., Runkel, F., Baader, S. L., Kappler, J., & Häberlein, H. (2004) · Biochemistry · doi:10.1021/bi035928t · Cited by 112

Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β 2 AR

Lamichhane, R., Liu, J. J., Pljevaljčić, G., White, K. L., der Schans, E. J. C. V., Katritch, V., Stevens, R. C., Wüthrich, K., & Millar, D. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519626112 · Cited by 111

Ligand Channeling within a G-protein-coupled Receptor

Schädel, S. A., Heck, M., Maretzki, D., Filipek, S., Teller, D. C., Palczewski, K., & Hofmann, K. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302115200 · Cited by 111

Pharmacology under the microscope: the use of fluorescence correlation spectroscopy to determine the properties of ligand–receptor complexes

Briddon, S. J., & Hill, S. J. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.09.008 · Cited by 110

Yeast Display Evolution of a Kinetically Efficient 13-Amino Acid Substrate for Lipoic Acid Ligase

Puthenveetil, S., Liu, D. S., White, K. A., Thompson, S., & Ting, A. Y. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904596f · Cited by 109

Conformation State-sensitive Antibodies to G-protein-coupled Receptors

Gupta, A., Décaillot, F. M., Gomes, I., Tkalych, O., Heimann, A. S., Ferro, E. S., & Devi, L. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609254200 · Cited by 109

The role of conformational ensembles of seven transmembrane receptors in functional selectivity

Vaidehi, N., & Kenakin, T. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.09.004 · Cited by 109

Fine tuning of sub-millisecond conformational dynamics controls metabotropic glutamate receptors agonist efficacy

Olofsson, L., Felekyan, S., Doumazane, E., Scholler, P., Fabre, L., Zwier, J. M., Rondard, P., Seidel, C. A. M., Pin, J., & Margeat, E. (2014) · Nature Communications · doi:10.1038/ncomms6206 · Cited by 108

A Genetically Encoded Acrylamide Functionality

Lee, Y., Wu, B., Raymond, J. E., Zeng, Y., Fang, X., Wooley, K. L., & Liu, W. R. (2013) · ACS Chemical Biology · doi:10.1021/cb400267m · Cited by 108

A fluorogenic ‘click’ reaction of azidoanthracene derivatives

Xie, F., Sivakumar, K., Zeng, Q., Bruckman, M. A., Hodges, B., & Wang, Q. (2008) · Tetrahedron · doi:10.1016/j.tet.2008.01.080 · Cited by 108

Rhodopsin Activation Exposes a Key Hydrophobic Binding Site for the Transducin α-Subunit C Terminus

Janz, J. M., & Farrens, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402567200 · Cited by 107

Novel Fluorophores for Single-Molecule Imaging

Willets, K. A., Ostroverkhova, O., He, M., Twieg, R. J., & Moerner, W. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029100q · Cited by 106

Principles of Single Molecule Multiparameter Fluorescence Spectroscopy

Kühnemuth, R., & Seidel, C. A. M. (2001) · Single Molecules · doi:10.1002/1438-5171(200112)2:4 · Cited by 106

Non-enzymatic Covalent Protein Labeling Using a Reactive Tag

Nonaka, H., Tsukiji, S., Ojida, A., & Hamachi, I. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074176d · Cited by 105

Distance Mapping in Proteins Using Fluorescence Spectroscopy: The Tryptophan-Induced Quenching (TrIQ) Method

Mansoor, S., DeWitt, M. A., & Farrens, D. (2010) · Biochemistry · doi:10.1021/bi100907m · Cited by 105

Probing Single Biomolecules in Solution Using the Anti-Brownian Electrokinetic (ABEL) Trap

Wang, Q., Goldsmith, R. H., Jiang, Y., Bockenhauer, S. D., & Moerner, W. E. (2012) · Accounts of Chemical Research · doi:10.1021/ar200304t · Cited by 104

Genetically encoding an aliphatic diazirine for protein photocrosslinking

Chou, C., Uprety, R., Davis, L., Chin, J. W., & Deiters, A. (2010) · Chemical Science · doi:10.1039/c0sc00373e · Cited by 104

Expanding the Genetic Code for Photoclick Chemistry in E. coli, Mammalian Cells, and A. thaliana

Li, F., Zhang, H., Sun, Y. W., Pan, Y., Zhou, J., & Wang, J. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303477 · Cited by 104

Asymmetry of GPCR oligomers supports their functional relevance

Maurice, P., Kamal, M., & Jockers, R. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.05.006 · Cited by 103

Single-molecule spectroscopy and imaging over the decades

Moerner, W. E., Shechtman, Y., & Wang, Q. (2015) · Faraday Discussions · doi:10.1039/c5fd00149h · Cited by 103

Single-molecule localization microscopy – near-molecular spatial resolution in light microscopy with photoswitchable fluorophores

Fürstenberg, A., & Heilemann, M. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp52289j · Cited by 103

Traceless Affinity Labeling of Endogenous Proteins for Functional Analysis in Living Cells

Hayashi, T., & Hamachi, I. (2012) · Accounts of Chemical Research · doi:10.1021/ar200334r · Cited by 101

Conformational Dynamics of Single G Protein-Coupled Receptors in Solution

Bockenhauer, S. D., Fürstenberg, A., Xiao, Y., Kobilka, B. K., & Moerner, W. E. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp204843r · Cited by 101

Imaging nanometer domains of β-adrenergic receptor complexes on the surface of cardiac myocytes

Ianoul, A. I., Grant, D. D., Rouleau, Y., Bani‐Yaghoub, M., Johnston, L. J., & Pezacki, J. P. (2005) · Nature Chemical Biology · doi:10.1038/nchembio726 · Cited by 101

Selective Covalent Labeling of Tag-Fused GPCR Proteins on Live Cell Surface with a Synthetic Probe for Their Functional Analysis

Nonaka, H., Fujishima, S., Uchinomiya, S., Ojida, A., & Hamachi, I. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910703v · Cited by 99

Heteromultimerization of Cannabinoid CB1 Receptor and Orexin OX1 Receptor Generates a Unique Complex in Which Both Protomers Are Regulated by Orexin A

Ward, R. J., Pediani, J. D., & Milligan, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287649 · Cited by 99

Fluorescence spectroscopy of rhodopsins: Insights and approaches

Alexiev, U., & Farrens, D. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.008 · Cited by 99

Correlated conformational events in EF-G and the ribosome regulate translocation

Munro, J. B., Wasserman, M. R., Altman, R. B., Wang, L., & Blanchard, S. C. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1925 · Cited by 99

Design Strategies for Bivalent Ligands Targeting GPCRs

Shonberg, J., Scammells, P. J., & Capuano, B. (2011) · ChemMedChem · doi:10.1002/cmdc.201100101 · Cited by 99

Adding value to fusion proteins through covalent labelling

Gronemeyer, T., Godin, G., & Johnsson, K. (2005) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2005.06.001 · Cited by 99

Fluorophore-tagged GPCR ligands

Middleton, R. J., & Kellam, B. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.016 · Cited by 99

Characterizing Molecular Interactions in Different Bacteriorhodopsin Assemblies by Single-molecule Force Spectroscopy

Sapra, K. T., Besir, H., Oesterhelt, D., & Müller, D. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.080 · Cited by 99

Rhodopsin self-associates in asolectin liposomes

Mansoor, S., Palczewski, K., & Farrens, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511010103 · Cited by 98

Visualizing odorant receptor trafficking in living cells down to the single-molecule level

Jacquier, V., Prummer, M., Segura, J., Pick, H. M., & Vogel, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603942103 · Cited by 97

Covalent agonists for studying G protein-coupled receptor activation

Weichert, D., Kruse, A. C., Manglik, A., Hiller, C., Zhang, C., Hübner, H., Kobilka, B. K., & Gmeiner, P. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410415111 · Cited by 97

Structural Features and Light-Dependent Changes in the Sequence 306−322 Extending from Helix VII to the Palmitoylation Sites in Rhodopsin: A Site-Directed Spin-Labeling Study,

Altenbach, C., Cai, K., Khorana, H. G., & Hubbell, W. L. (1999) · Biochemistry · doi:10.1021/bi9900121 · Cited by 97

Solubilization, stabilization, and purification of chemokine receptors using biosensor technology

Navratilova, I. H., Sodroski, J., & Myszka, D. G. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2004.12.017 · Cited by 96

An Engineered Aryl Azide Ligase for Site‐Specific Mapping of Protein–Protein Interactions through Photo‐Cross‐Linking

Baruah, H., Puthenveetil, S., Choi, Y., Shah, S., & Ting, A. Y. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802088 · Cited by 95

Progress Toward an Expanded Eukaryotic Genetic Code

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Ligand-Specific Interactions Modulate Kinetic, Energetic, and Mechanical Properties of the Human β2 Adrenergic Receptor

Zocher, M., Fung, J. J., Kobilka, B. K., & Müller, D. J. (2012) · Structure · doi:10.1016/j.str.2012.05.010 · Cited by 94

Fluorescent ligand binding reveals heterogeneous distribution of adrenoceptors and ‘cannabinoid‐like’ receptors in small arteries

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New Fluorescent Adenosine A1-Receptor Agonists That Allow Quantification of Ligand−Receptor Interactions in Microdomains of Single Living Cells

Middleton, R. J., Briddon, S. J., Cordeaux, Y., Yates, A. S., Dale, C. L., George, M. W., Baker, J. G., Hill, S. J., & Kellam, B. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061279i · Cited by 93

A Genetically Encoded Diazirine Photocrosslinker in Escherichia coli

Tippmann, E. M., Liu, W. R., Summerer, D., Mack, A. V., & Schultz, P. G. (2007) · ChemBioChem · doi:10.1002/cbic.200700460 · Cited by 93

The Beginnings of Immunofluorescence

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Cell Type-specific β2-Adrenergic Receptor Clusters Identified Using Photoactivated Localization Microscopy Are Not Lipid Raft Related, but Depend on Actin Cytoskeleton Integrity

Scarselli, M., Annibale, P., & Rađenović, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329912 · Cited by 92

New Aldehyde Tag Sequences Identified by Screening Formylglycine Generating Enzymes in Vitro and in Vivo

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Demonstration of Improvements to the Bioluminescence Resonance Energy Transfer (BRET) Technology for the Monitoring of G Protein–Coupled Receptors in Live Cells

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A Fluorogenic TMP-Tag for High Signal-to-Background Intracellular Live Cell Imaging

Jing, C., & Cornish, V. W. (2013) · ACS Chemical Biology · doi:10.1021/cb300657r · Cited by 91

Twenty-first aminoacyl-tRNA synthetase–suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

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Genetic code expansion enabled site-specific dual-color protein labeling: superresolution microscopy and beyond

Nikić, I., & Lemke, E. A. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.07.021 · Cited by 89

Strain-Promoted Oxidation-Controlled Cyclooctyne–1,2-Quinone Cycloaddition (SPOCQ) for Fast and Activatable Protein Conjugation

Borrmann, A., Fatunsin, O., Dommerholt, J., Jonker, A. M., Löwik, D. W. P. M., van Hest, J. C. M., & van Delft, F. L. (2014) · Bioconjugate Chemistry · doi:10.1021/bc500534d · Cited by 89

When a G protein-coupled receptor does not couple to a G protein

Sun, Y., McGarrigle, D. K., & Huang, X.-Y. (2007) · Molecular BioSystems · doi:10.1039/b706343a · Cited by 88

A Brief History of Great Discoveries in Pharmacology: In Celebration of the Centennial Anniversary of the Founding of the American Society of Pharmacology and Experimental Therapeutics

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Site-Specific Incorporation of Photo-Cross-Linker and Bioorthogonal Amino Acids into Enteric Bacterial Pathogens

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Single-molecule spectroscopy of the β 2 adrenergic receptor: Observation of conformational substates in a membrane protein

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Homogeneous time-resolved fluorescence-based assay to screen for ligands targeting the growth hormone secretagogue receptor type 1a

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Signaling through a G Protein-coupled Receptor and Its Corresponding G Protein Follows a Stoichiometrically Limited Model

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Single-molecule imaging of Hedgehog pathway protein Smoothened in primary cilia reveals binding events regulated by Patched1

Milenković, L., Weiss, L. E., Yoon, J., Roth, T. L., Su, Y. S., Sahl, S. J., Scott, M. P., & Moerner, W. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510094112 · Cited by 85

Solution 19 F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin

Loewen, M. C., Klein‐Seetharaman, J., Getmanova, E. V., Reeves, P. J., Schwalbe, H., & Khorana, H. G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051633098 · Cited by 85

Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex

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Structural Features and Light-Dependent Changes in the Sequence 59−75 Connecting Helices I and II in Rhodopsin: A Site-Directed Spin-Labeling Study ,

Altenbach, C., Klein‐Seetharaman, J., Hwa, J., Khorana, H. G., & Hubbell, W. L. (1999) · Biochemistry · doi:10.1021/bi990014l · Cited by 84

Structure and Function in Rhodopsin. Single Cysteine Substitution Mutants in the Cytoplasmic Interhelical E−F Loop Region Show Position-Specific Effects in Transducin Activation

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Effect of channel mutations on the uptake and release of the retinal ligand in opsin

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Altered surface trafficking of presynaptic cannabinoid type 1 receptor in and out synaptic terminals parallels receptor desensitization

Mikasová, L., Groc, L., Choquet, D., & Manzoni, O. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805959105 · Cited by 82

Illuminating the life of GPCRs

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LDAI-Based Chemical Labeling of Intact Membrane Proteins and Its Pulse-Chase Analysis under Live Cell Conditions

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Yeast suppressors of UAA and UAG nonsense codons work efficiently in vitro via tRNA

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Genetically Encoding Unnatural Amino Acids in Neural Stem Cells and Optically Reporting Voltage-Sensitive Domain Changes in Differentiated Neurons

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Probing the role of the cation–π interaction in the binding sites of GPCRs using unnatural amino acids

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Peptide‐Templated Acyl Transfer: A Chemical Method for the Labeling of Membrane Proteins on Live Cells

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Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution

Jiang, Y., Douglas, N. R., Conley, N. R., Miller, E. J., Frydman, J., & Moerner, W. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112244108 · Cited by 79

Oligomer Size of the Serotonin 5-Hydroxytryptamine 2C (5-HT2C) Receptor Revealed by Fluorescence Correlation Spectroscopy with Photon Counting Histogram Analysis

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