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

VMD: visual molecular dynamics

Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952

Imaging Intracellular Fluorescent Proteins at Nanometer Resolution

Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S. G., Bonifacino, J. S., Davidson, M. W., Lippincott‐Schwartz, J., & Hess, H. F. (2006) · Science · doi:10.1126/science.1127344 · Cited by 8,941

Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)

Rust, M., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 7,823

Green fluorescent protein as a marker for gene expression

Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., & Prasher, D. C. (1994) · Science · doi:10.1126/science.8303295 · Cited by 6,802

Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy

Hell, S. W., & Wichmann, J. (1994) · Optics Letters · doi:10.1364/ol.19.000780 · Cited by 6,068

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637

Cu-Catalyzed Azide−Alkyne Cycloaddition

Meldal, M., & Tornøe, C. W. (2008) · Chemical Reviews · doi:10.1021/cr0783479 · Cited by 4,780

Thiol–Ene Click Chemistry

Hoyle, C. E., & Bowman, C. N. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200903924 · Cited by 4,201

Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy

Hess, S. T., Girirajan, T. P. K., & Mason, M. D. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.091116 · Cited by 3,684

How many drug targets are there?

Overington, J. P., Al-Lazikani, B., & Hopkins, A. L. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2199 · Cited by 3,505

High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Kühn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,280

The Energy Landscapes and Motions of Proteins

Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250

Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality

Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165

A Strain-Promoted [3 + 2] Azide−Alkyne Cycloaddition for Covalent Modification of Biomolecules in Living Systems

Agard, N. J., Prescher, J. A., & Bertozzi, C. R. (2004) · Journal of the American Chemical Society · doi:10.1021/ja044996f · Cited by 3,160

Crystal structure of the β2 adrenergic receptor–Gs protein complex

Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009

Far-field optical nanoscopy

Hell, S. W. (2007) · Science · doi:10.1126/science.1137395 · Cited by 2,967

A guide to choosing fluorescent proteins

Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005) · Nature Methods · doi:10.1038/nmeth819 · Cited by 2,823

The Fluorescent Toolbox for Assessing Protein Location and Function

Giepmans, B. N. G., Adams, S., Ellisman, M. H., & Tsien, R. Y. (2006) · Science · doi:10.1126/science.1124618 · Cited by 2,782

HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis

Los, G. V., Encell, L. P., McDougall, M. G., Hartzell, D. D., Karassina, N., Zimprich, C., Wood, M. G., Learish, R., Ohana, R. F., Urh, M., et al. (2008) · ACS Chemical Biology · doi:10.1021/cb800025k · Cited by 2,624

Dynamic personalities of proteins

Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545

The structure and function of G-protein-coupled receptors

Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534

Cell Surface Engineering by a Modified Staudinger Reaction

Saxon, E., & Bertozzi, C. R. (2000) · Science · doi:10.1126/science.287.5460.2007 · Cited by 2,463

A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells

Roux, K. J., Kim, D. I., Raida, M., & Burke, B. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201112098 · Cited by 2,416

Fluorescence Energy Transfer as a Spectroscopic Ruler

Stryer, L. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.004131 · Cited by 2,416

A practical guide to single-molecule FRET

Roy, R., Hohng, S., & Ha, T. (2008) · Nature Methods · doi:10.1038/nmeth.1208 · Cited by 2,174

Fluorescence Spectroscopy of Single Biomolecules

Weiss, S. (1999) · Science · doi:10.1126/science.283.5408.1676 · Cited by 2,060

Free radical-mediated oxidation of free amino acids and amino acid residues in proteins

Stadtman, E. R., & Levine, R. L. (2003) · Amino Acids · doi:10.1007/s00726-003-0011-2 · Cited by 1,968

A general method for the covalent labeling of fusion proteins with small molecules in vivo

Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H. M., Vogel, H., & Johnsson, K. (2002) · Nature Biotechnology · doi:10.1038/nbt765 · Cited by 1,964

Semiconductor Nanocrystals: Structure, Properties, and Band Gap Engineering

Smith, A. M., & Nie, S. (2009) · Accounts of Chemical Research · doi:10.1021/ar9001069 · Cited by 1,944

Crystal structure of the human β2 adrenergic G-protein-coupled receptor

Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935

Azobenzene photoswitches for biomolecules

Beharry, A. A., & Woolley, G. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15023e · Cited by 1,884

Subdiffraction‐Resolution Fluorescence Imaging with Conventional Fluorescent Probes

Heilemann, M., van de Linde, S., Schüttpelz, M., Kasper, R. T., Seefeldt, B., Mukherjee, A., Tinnefeld, P., & Sauer, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802376 · Cited by 1,870

Wavelength mutations and posttranslational autoxidation of green fluorescent protein.

Heim, R., Prasher, D. C., & Tsien, R. Y. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12501 · Cited by 1,857

SINGLE-PARTICLE TRACKING:Applications to Membrane Dynamics

Saxton, M. J., & Jacobson, K. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.373 · Cited by 1,810

The 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist

Jaakola, V., Griffith, M. T., Hanson, M. A., Cherezov, V., Chien, E. Y. T., Lane, J. R., IJzerman, A. P., & Stevens, R. C. (2008) · Science · doi:10.1126/science.1164772 · Cited by 1,786

Adding New Chemistries to the Genetic Code

Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725

Structure of a nanobody-stabilized active state of the β2 adrenoceptor

Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,709

Cu-free click cycloaddition reactions in chemical biology

Jewett, J. C., & Bertozzi, C. R. (2010) · Chemical Society Reviews · doi:10.1039/b901970g · Cited by 1,684

Bioconjugation by Copper(I)-Catalyzed Azide-Alkyne [3 + 2] Cycloaddition

Wang, Q., Chan, T. R., Hilgraf, R., Fokin, V. V., Sharpless, K. B., & Finn, M. G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja021381e · Cited by 1,638

Dimerization of cell surface receptors in signal transduction

Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634

The molecular structure of green fluorescent protein

Yang, F., Moss, L. G., & Phillips, G. N. (1996) · Nature Biotechnology · doi:10.1038/nbt1096-1246 · Cited by 1,580

Specific Covalent Labeling of Recombinant Protein Molecules Inside Live Cells

Griffin, B. A., Adams, S., & Tsien, R. Y. (1998) · Science · doi:10.1126/science.281.5374.269 · Cited by 1,580

Structural diversity of G protein-coupled receptors and significance for drug discovery

Lagerström, M. C., & Schiöth, H. B. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2518 · Cited by 1,557

Molecular tinkering of G protein‐coupled receptors: an evolutionary success

Bockaert, J., & Pin, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1723 · Cited by 1,548

Molecular signatures of G-protein-coupled receptors

Venkatakrishnan, A., Deupí, X., Lebon, G., Tate, C. G., Schertler, G. F. X., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,534

Expanding the Genetic Code of Escherichia coli

Wang, L., Brock, A., Herberich, B., & Schultz, P. G. (2001) · Science · doi:10.1126/science.1060077 · Cited by 1,504

Chemistry in living systems

Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,473

Diffusion Dynamics of Glycine Receptors Revealed by Single-Quantum Dot Tracking

Dahan, M., Lévi, S., Luccardini, C., Rostaing, P., Riveau, B., & Triller, A. (2003) · Science · doi:10.1126/science.1088525 · Cited by 1,465

OXIDATION OF FREE AMINO ACIDS AND AMINO ACID RESIDUES IN PROTEINS BY RADIOLYSIS AND BY METAL-CATALYZED REACTIONS

Stadtman, E. R. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004053 · Cited by 1,408

Crystal structure of the µ-opioid receptor bound to a morphinan antagonist

Manglik, A., Kruse, A. C., Kobilka, T. S., Thian, F. S., Mathiesen, J. M., Sunahara, R. K., Pardo, L., Weis, W. I., Kobilka, B. K., & Granier, S. (2012) · Nature · doi:10.1038/nature10954 · Cited by 1,400

β-Arrestins and Cell Signaling

DeWire, S. M., Ahn, S., Lefkowitz, R. J., & Shenoy, S. K. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.022405.154749 · Cited by 1,397

Directed evolution of APEX2 for electron microscopy and proximity labeling

Lam, S. S., Martell, J. D., Kamer, K. J., Deerinck, T. J., Ellisman, M. H., Mootha, V. K., & Ting, A. Y. (2014) · Nature Methods · doi:10.1038/nmeth.3179 · Cited by 1,395

Quantum Dots as Cellular Probes

Alivisatos, A. P., Gu, W., & Larabell, C. A. (2005) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.7.060804.100432 · Cited by 1,368

Understanding, improving and using green fluorescent proteins

Cubitt, A. B., Heim, R., Adams, S., Boyd, A. E., Gross, L. A., & Tsien, R. Y. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89099-4 · Cited by 1,352

GPCR Engineering Yields High-Resolution Structural Insights into β 2 -Adrenergic Receptor Function

Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Yao, X.-J., Weis, W. I., Stevens, R. C., et al. (2007) · Science · doi:10.1126/science.1150609 · Cited by 1,335

Proteomic Mapping of Mitochondria in Living Cells via Spatially Restricted Enzymatic Tagging

Martell, J. D., Ting, A. Y., Rhee, H., Zou, P., Udeshi, N. D., Mootha, V. K., & Carr, S. A. (2012) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 1,330

Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin

Dixon, R. A. F., Kobilka, B. K., Strader, D. J., Benovic, J., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., et al. (1986) · Nature · doi:10.1038/321075a0 · Cited by 1,275

Optical detection and spectroscopy of single molecules in a solid

Moerner, W. E., & Kador, L. (1989) · Physical Review Letters · doi:10.1103/physrevlett.62.2535 · Cited by 1,273

Single Molecules Observed by Near-Field Scanning Optical Microscopy

Betzig, E., & Chichester, R. J. (1993) · Science · doi:10.1126/science.262.5138.1422 · Cited by 1,266

Codon usage tabulated from international DNA sequence databases: status for the year 2000

Nakamura, Y. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.292 · Cited by 1,259

Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor.

Ha, T., Enderle, T., Ogletree, D. F., Chemla, D. S., Selvin, P. R., & Weiss, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6264 · Cited by 1,247

Heterotrimeric G protein activation by G-protein-coupled receptors

Oldham, W. M., & Hamm, H. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2299 · Cited by 1,234

Biomolecular Simulation: A Computational Microscope for Molecular Biology

Dror, R. O., Dirks, R. M., Grossman, J. P., Xu, H., & Shaw, D. E. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155245 · Cited by 1,226

Fluorescent Labeling of Biomolecules with Organic Probes

Gonçalves, M. S. T. (2008) · Chemical Reviews · doi:10.1021/cr0783840 · Cited by 1,188

Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

Farrens, D., Altenbach, C., Yang, K., Hubbell, W. L., & Khorana, H. G. (1996) · Science · doi:10.1126/science.274.5288.768 · Cited by 1,179

Cyclic GMP Cascade of Vision

Stryer, L. (1986) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.09.030186.000511 · Cited by 1,172

Illuminating Single Molecules in Condensed Matter

Moerner, W. E., & Orrit, M. (1999) · Science · doi:10.1126/science.283.5408.1670 · Cited by 1,143

Advances in Chemical Protein Modification

Boutureira, O., & Bernardes, G. J. L. (2015) · Chemical Reviews · doi:10.1021/cr500399p · Cited by 1,137

An Engineered Protein Tag for Multiprotein Labeling in Living Cells

Gautier, A., Juillerat, A., Heinis, C., Junior, I. R. C., Kindermann, M., Beaufils, F., & Johnsson, K. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.01.007 · Cited by 1,119

Structure-Function of the G Protein–Coupled Receptor Superfamily

Katritch, V., Cherezov, V., & Stevens, R. C. (2012) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-032112-135923 · Cited by 1,096

From Mechanism to Mouse: A Tale of Two Bioorthogonal Reactions

Sletten, E. M., & Bertozzi, C. R. (2011) · Accounts of Chemical Research · doi:10.1021/ar200148z · Cited by 1,095

Crystal structure of opsin in its G-protein-interacting conformation

Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059

Cellular Incorporation of Unnatural Amino Acids and Bioorthogonal Labeling of Proteins

Lang, K., & Chin, J. W. (2014) · Chemical Reviews · doi:10.1021/cr400355w · Cited by 1,051

The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure

Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049

A General Method for Site-specific Incorporation of Unnatural Amino Acids into Proteins

Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., & Schultz, P. G. (1989) · Science · doi:10.1126/science.2649980 · Cited by 1,019

Conformational Substates in Proteins

Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 995

Circular permutation and receptor insertion within green fluorescent proteins

Baird, G. S., Zacharias, D. A., & Tsien, R. Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11241 · Cited by 963

Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein

Cabantous, S., Terwilliger, T. C., & Waldo, G. S. (2004) · Nature Biotechnology · doi:10.1038/nbt1044 · Cited by 957

New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo: Synthesis and Biological Applications

Adams, S., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., & Tsien, R. Y. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017687n · Cited by 947

Visualizing Metabolically Labeled Glycoconjugates of Living Cells by Copper‐Free and Fast Huisgen Cycloadditions

Ning, X., Guo, J., Wolfert, M. A., & Boons, G. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705456 · Cited by 925

Structural insights into µ-opioid receptor activation

Huang, W., Manglik, A., Venkatakrishnan, A., Laeremans, T., Feinberg, E. N., Sanborn, A. L., KATO, H. E., Livingston, K. E., Thorsen, T. S., Kling, R. C., et al. (2015) · Nature · doi:10.1038/nature14886 · Cited by 920

A near-infrared fluorophore for live-cell super-resolution microscopy of cellular proteins

Lukinavičius, G., Umezawa, K., Olivier, N., Honigmann, A., Yang, G., Plass, T., Mueller, V., Reymond, L., Junior, I. R. C., Luo, Z., et al. (2013) · Nature Chemistry · doi:10.1038/nchem.1546 · Cited by 911

Crystal structure of the ligand-free G-protein-coupled receptor opsin

Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 908

Activation and allosteric modulation of a muscarinic acetylcholine receptor

Kruse, A. C., Ring, A. M., Manglik, A., Hu, J., Hu, K., Eitel, K., Hübner, H., Pardon, E., Valant, C., Sexton, P. M., et al. (2013) · Nature · doi:10.1038/nature12735 · Cited by 902

Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation

Lebon, G., Warne, T., Edwards, P. C., Bennett, K. A., Langmead, C. J., Leslie, A. G. W., & Tate, C. G. (2011) · Nature · doi:10.1038/nature10136 · Cited by 892

Methods of single-molecule fluorescence spectroscopy and microscopy

Moerner, W. E., & Fromm, D. P. (2003) · Review of Scientific Instruments · doi:10.1063/1.1589587 · Cited by 888

Receptors for Dopamine and Somatostatin: Formation of Hetero-Oligomers with Enhanced Functional Activity

Rocheville, M., Lange, D. C., Kumar, U., Patel, S. C., Patel, R. C., & Patel, Y. (2000) · Science · doi:10.1126/science.288.5463.154 · Cited by 887

Trends in the exploitation of novel drug targets

Rask-Andersen, M., Almén, M. S., & Schiöth, H. B. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3478 · Cited by 853

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Yang, H., Luo, G., Karnchanaphanurach, P., Louie, T. M., Rech, I., Cova, S., Xun, L., & Xie, X. S. (2003) · Science · doi:10.1126/science.1086911 · Cited by 841

Structure and dynamics of the M3 muscarinic acetylcholine receptor

Kruse, A. C., Hu, J., Pan, A. C., Arlow, D. H., Rosenbaum, D. M., Rosemond, E., Green, H. F., Liu, T., Chae, P. S., Dror, R. O., et al. (2012) · Nature · doi:10.1038/nature10867 · Cited by 836

Structure of an Agonist-Bound Human A 2A Adenosine Receptor

Xu, F., Wu, H., Katritch, V., Han, G. W., Jacobson, K. A., Gao, Z., Cherezov, V., & Stevens, R. C. (2011) · Science · doi:10.1126/science.1202793 · Cited by 820

An Expanded Eukaryotic Genetic Code

Chin, J. W., Cropp, T. A., Anderson, J. C., Mukherji, M., Zhang, Z., & Schultz, P. G. (2003) · Science · doi:10.1126/science.1084772 · Cited by 820

Conformational biosensors reveal GPCR signalling from endosomes

Irannejad, R., Tomshine, J. C., Tomshine, J. R., Chevalier, M., Mahoney, J. P., Steyaert, J., Rasmussen, S. G. F., Sunahara, R. K., El-Samad, H., Huang, B., et al. (2013) · Nature · doi:10.1038/nature12000 · Cited by 819

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Kang, Y., Zhou, X. E., Gao, X., He, Y., Liu, W., Ishchenko, A., Barty, A., White, T. A., Yefanov, O. M., Han, G. W., et al. (2015) · Nature · doi:10.1038/nature14656 · Cited by 818

The Dynamic Process of β2-Adrenergic Receptor Activation

Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.008 · Cited by 815

Cloning, Sequencing, and Expression of the Gene Coding for the Human Platelet α 2 -Adrenergic Receptor

Kobilka, B. K., Matsui, H., Kobilka, T. S., Yang‐Feng, T. L., Francke, U., Caron, M. G., Lefkowitz, R. J., & Regan, J. W. (1987) · Science · doi:10.1126/science.2823383 · Cited by 786

Structure and function of an irreversible agonist-β2 adrenoceptor complex

Rosenbaum, D. M., Zhang, C., Lyons, J. A., Holl, R., Aragão, D., Arlow, D. H., Rasmussen, S. G. F., Choi, H., DeVree, B. T., Sunahara, R. K., et al. (2011) · Nature · doi:10.1038/nature09665 · Cited by 771

Projection structure of rhodopsin

Schertler, G. F. X., Villa, C., & Henderson, R. A. (1993) · Nature · doi:10.1038/362770a0 · Cited by 766

Signalling bias in new drug discovery: detection, quantification and therapeutic impact

Kenakin, T., & Christopoulos, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3954 · Cited by 764

Chimeric α 2 -,β 2 -Adrenergic Receptors: Delineation of Domains Involved in Effector Coupling and Ligand Binding Specificity

Kobilka, B. K., Kobilka, T. S., Daniel, K. W., Regan, J. W., Caron, M. G., & Lefkowitz, R. J. (1988) · Science · doi:10.1126/science.2836950 · Cited by 763

Rhodopsin dimers in native disc membranes

Fotiadis, D., Liang, Y., Filipek, S., Saperstein, D. A., Engel, A., & Palczewski, K. (2003) · Nature · doi:10.1038/421127a · Cited by 749

A Comparative Study of Bioorthogonal Reactions with Azides

Agard, N. J., Baskin, J. M., Prescher, J. A., Lo, A., & Bertozzi, C. R. (2006) · ACS Chemical Biology · doi:10.1021/cb6003228 · Cited by 744

Structure of Bovine Rhodopsin in a Trigonal Crystal Form

Li, J., Edwards, P. C., Burghammer, M. C., Villa, C., & Schertler, G. F. X. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.090 · Cited by 724

Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy

Martell, J. D., Deerinck, T. J., Sancak, Y., Poulos, T. L., Mootha, V. K., Sosinsky, G. E., Ellisman, M. H., & Ting, A. Y. (2012) · Nature Biotechnology · doi:10.1038/nbt.2375 · Cited by 722

Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)

Angers, S., Salahpour, A., Joly, E., Hilairet, S., Chelsky, D., Dennis, M., & Bouvier, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3684 · Cited by 721

Advances in Single-Molecule Fluorescence Methods for Molecular Biology

Joo, C., Balci, H., Ishitsuka, Y., Buranachai, C., & Ha, T. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.070606.101543 · Cited by 718

Structure of the CCR5 Chemokine Receptor–HIV Entry Inhibitor Maraviroc Complex

Tan, Q., Zhu, Y., Li, J., Chen, Z., Han, G. W., Kufareva, I., Li, T., Ma, L., Fenalti, G., Li, J., et al. (2013) · Science · doi:10.1126/science.1241475 · Cited by 710

Regulation of Receptor Trafficking by GRKs and Arrestins

Moore, C. A. C., Milano, S. K., & Benovic, J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.022405.154712 · Cited by 709

Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR

Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., & Wüthrich, K. (2012) · Science · doi:10.1126/science.1215802 · Cited by 706

A Fluorogenic 1,3-Dipolar Cycloaddition Reaction of 3-Azidocoumarins and Acetylenes

Sivakumar, K., Xie, F., Cash, B. M., Long, S., Barnhill, H. N., & Wang, Q. (2004) · Organic Letters · doi:10.1021/ol047955x · Cited by 700

Conformational complexity of G-protein-coupled receptors

Kobilka, B. K., & Deupí, X. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.003 · Cited by 694

Subunit counting in membrane-bound proteins

Ulbrich, M. H., & Isacoff, E. Y. (2007) · Nature Methods · doi:10.1038/nmeth1024 · Cited by 693

Photophysics of Fluorescent Probes for Single-Molecule Biophysics and Super-Resolution Imaging

Ha, T., & Tinnefeld, P. (2012) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-032210-103340 · Cited by 692

A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein

Whorton, M. R., Bokoch, M. P., Rasmussen, S. G. F., Huang, B., Zare, R. N., Kobilka, B. K., & Sunahara, R. K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611448104 · Cited by 686

Roles of G‐protein‐coupled receptor dimerization

Terrillon, S., & Bouvier, M. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400052 · Cited by 684

A Trafficking Checkpoint Controls GABAB Receptor Heterodimerization

Margeta, M., Jan, Y. N., & Jan, L. Y. (2000) · Neuron · doi:10.1016/s0896-6273(00)00012-x · Cited by 680

Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling

Manglik, A., Kim, T. H., Masureel, M., Altenbach, C., Yang, Z., Hilger, D., Lerch, M. T., Kobilka, T. S., Thian, F. S., Hubbell, W. L., et al. (2015) · Cell · doi:10.1016/j.cell.2015.04.043 · Cited by 671

Oligomerization of G-protein-coupled transmitter receptors

Bouvier, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35067575 · Cited by 668

Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase

Chen, I., Howarth, M. R., Lin, W., & Ting, A. Y. (2005) · Nature Methods · doi:10.1038/nmeth735 · Cited by 668

Crystal structure of metarhodopsin II

Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663

Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules

Kapanidis, A. N., Lee, N. K., Laurence, T. A., Doose, S., Margeat, E., & Weiss, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401690101 · Cited by 631

Activation mechanism of the β 2 -adrenergic receptor

Dror, R. O., Arlow, D. H., Maragakis, P., Mildorf, T. J., Pan, A. C., Xu, H., Borhani, D. W., & Shaw, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110499108 · Cited by 629

Pyrrolysine Encoded by UAG in Archaea: Charging of a UAG-Decoding Specialized tRNA

Srinivasan, G., James, C. M., & Krzycki, J. A. (2002) · Science · doi:10.1126/science.1069588 · Cited by 629

A family of receptors coupled to guanine nucleotide regulatory proteins

Dohlman, H. G., Caron, M. G., & Lefkowitz, R. J. (1987) · Biochemistry · doi:10.1021/bi00384a001 · Cited by 626

Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome

Neumann, H., Wang, K., Davis, L., Garcia-Alai, M., & Chin, J. W. (2010) · Nature · doi:10.1038/nature08817 · Cited by 622

Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3.

Zhouravleva, G. A., FROLOVA, L. Y., Goff, X. L., Guellec, R. L., Inge-Vechtomov, S. G., Kisselev, L. L., & Philippe, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00078.x · Cited by 610

Poly(ethylene oxide) Grafted to Silicon Surfaces: Grafting Density and Protein Adsorption

Sofia, S. J., Premnath, V., & Merrill, E. W. (1998) · Macromolecules · doi:10.1021/ma971016l · Cited by 610

Regulation of GPCRs by Endocytic Membrane Trafficking and Its Potential Implications

Hanyaloglu, A. C., & von Zastrow, M. (2007) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094830 · Cited by 610

β-Arrestin-biased ligands at seven-transmembrane receptors

Violin, J. D., & Lefkowitz, R. J. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.006 · Cited by 606

Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs),

Teller, D. C., Okada, T., Behnke, C. A., Palczewski, K., & Stenkamp, R. E. (2001) · Biochemistry · doi:10.1021/bi0155091 · Cited by 603

Organization of the G Protein-coupled Receptors Rhodopsin and Opsin in Native Membranes

Liang, Y., Fotiadis, D., Filipek, S., Saperstein, D. A., Palczewski, K., & Engel, A. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302536200 · Cited by 595

G-Protein-coupled receptor oligomerization and its potential for drug discovery

George, S. R., O’Dowd, B. F., & Lee, S. P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd913 · Cited by 590

Mitochondrial CB1 receptors regulate neuronal energy metabolism

Bénard, G., Massa, F., Puente, N., Lourenço, J., Bellocchio, L., Soria-Gómez, E., Matias, I., Delamarre, A., Metna-Laurent, M., Cannich, A., et al. (2012) · Nature Neuroscience · doi:10.1038/nn.3053 · Cited by 588

Dimerization: An Emerging Concept for G Protein–Coupled Receptor Ontogeny and Function

Angers, S., Salahpour, A., & Bouvier, M. (2002) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.091701.082314 · Cited by 587

EXPANDING THE GENETIC CODE

Wang, L., Xie, J., & Schultz, P. G. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.101105.121507 · Cited by 584

Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors

Reiter, É., Ahn, S., Shukla, A. K., & Lefkowitz, R. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105800 · Cited by 582

Cloning of the cDNA for the human beta 1-adrenergic receptor.

Frielle, T., Collins, S., Daniel, K. W., Caron, M. G., Lefkowitz, R. J., & Kobilka, B. K. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.7920 · Cited by 575

G Protein–Coupled Receptor Oligomerization Revisited: Functional and Pharmacological Perspectives

Ferré, S., Casadó, V., Devi, L. A., Filizola, M., Jockers, R., Lohse, M. J., Milligan, G., Pin, J., & Guitart, X. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.008052 · Cited by 574

Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)

Pfleger, K. D. G., & Eidne, K. A. (2006) · Nature Methods · doi:10.1038/nmeth841 · Cited by 571

Oxidative Stress and Covalent Modification of Protein with Bioactive Aldehydes

Grimsrud, P. A., Xie, H., Griffin, T. J., & Bernlohr, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700019200 · Cited by 570

Spatially resolved proteomic mapping in living cells with the engineered peroxidase APEX2

Hung, V., Udeshi, N. D., Lam, S. S., Loh, K. H., Cox, K. J., Pedram, K., Carr, S. A., & Ting, A. Y. (2016) · Nature Protocols · doi:10.1038/nprot.2016.018 · Cited by 569

Bioorthogonal Reactions for Labeling Proteins

Lang, K., & Chin, J. W. (2014) · ACS Chemical Biology · doi:10.1021/cb4009292 · Cited by 566

Bioconjugation with Strained Alkenes and Alkynes

Debets, M. F., van Berkel, S. S., Dommerholt, J., Dirks, A. J., Rutjes, F. P. J. T., & van Delft, F. L. (2011) · Accounts of Chemical Research · doi:10.1021/ar200059z · Cited by 565

Principles and Biophysical Applications of Lanthanide-Based Probes

Selvin, P. R. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.101101.140927 · Cited by 549

Fluorescence Correlation Spectroscopy: Novel Variations of an Established Technique

Haustein, E., & Schwille, P. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132612 · Cited by 548

Targeting quantum dots to surface proteins in living cells with biotin ligase

Howarth, M. R., Takao, K., Hayashi, Y., & Ting, A. Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503125102 · Cited by 544

Superresolution Imaging using Single-Molecule Localization

Patterson, G. H., Davidson, M. W., Manley, S., & Lippincott‐Schwartz, J. (2010) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.012809.103444 · Cited by 544

Sortagging: a versatile method for protein labeling

Popp, M. W., Antos, J. M., Grotenbreg, G. M., Spooner, E., & Ploegh, H. L. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.31 · Cited by 542

Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules

Doose, S., Neuweiler, H., & Sauer, M. (2009) · ChemPhysChem · doi:10.1002/cphc.200900238 · Cited by 535

Single-Molecule Fluorescence Studies of Protein Folding and Conformational Dynamics

Michalet, X., Weiss, S., & Jäger, M. (2006) · Chemical Reviews · doi:10.1021/cr0404343 · Cited by 533

Genetic Encoding of Bicyclononynes and trans-Cyclooctenes for Site-Specific Protein Labeling in Vitro and in Live Mammalian Cells via Rapid Fluorogenic Diels–Alder Reactions

Lang, K., Davis, L., Wallace, S., Mahesh, M., Cox, D. J., Blackman, M. L., Fox, J. M., & Chin, J. W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302832g · Cited by 529

Subtypes of the Somatostatin Receptor Assemble as Functional Homo- and Heterodimers

Rocheville, M., Lange, D. C., Kumar, U., Sasi, R., Patel, R. C., & Patel, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7862 · Cited by 527

The structure of bovine rhodopsin

Hargrave, P. A., McDowell, J. H., Curtis, D. R., Wang, J. K., Juszczak, E., Fong, S., Rao, J., & Argos, P. (1983) · European Biophysics Journal · doi:10.1007/bf00535659 · Cited by 519

Biomedical Applications of Tetrazine Cycloadditions

Devaraj, N. K., & Weissleder, R. (2011) · Accounts of Chemical Research · doi:10.1021/ar200037t · Cited by 519

Proteomic Mapping of the Human Mitochondrial Intermembrane Space in Live Cells via Ratiometric APEX Tagging

Hung, V., Zou, P., Rhee, H.-W., Udeshi, N. D., Cracan, V., Svinkina, T., Carr, S. A., Mootha, V. K., & Ting, A. Y. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.003 · Cited by 517

Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications

Young, C. L., Britton, Z. T., & Robinson, A. S. (2012) · Biotechnology Journal · doi:10.1002/biot.201100155 · Cited by 507

Visualization of arrestin recruitment by a G-protein-coupled receptor

Shukla, A. K., Westfield, G., Xiao, K., Reis, R. I., Huang, L.-Y., Tripathi‐Shukla, P., Qian, J. X., Li, S., Blanc, A., Oleskie, A. N., et al. (2014) · Nature · doi:10.1038/nature13430 · Cited by 503

The Crystal Structure of Human Eukaryotic Release Factor eRF1—Mechanism of Stop Codon Recognition and Peptidyl-tRNA Hydrolysis

Song, H., Mugnier, P., Das, A. K., Webb, H., Evans, D. R., Tuite, M. F., Hemmings, B. A., & Barford, D. (2000) · Cell · doi:10.1016/s0092-8674(00)80667-4 · Cited by 501

Adrenaline-activated structure of β2-adrenoceptor stabilized by an engineered nanobody

Ring, A. M., Manglik, A., Kruse, A. C., Enos, M. D., Weis, W. I., García, K. C., & Kobilka, B. K. (2013) · Nature · doi:10.1038/nature12572 · Cited by 500

Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization

Maurel, D., Comps‐Agrar, L., Brock, C., Rives, M., Bourrier, E., Ayoub, M. A., Bazin, H., Tinel, N., Durroux, T., Prézeau, L., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1213 · Cited by 500

Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction

Lang, K., Davis, L., Torres‐Kolbus, J., Chou, C., Deiters, A., & Chin, J. W. (2012) · Nature Chemistry · doi:10.1038/nchem.1250 · Cited by 488

A FlAsH-based FRET approach to determine G protein–coupled receptor activation in living cells

Hoffmann, C., Gaietta, G. M., Bünemann, M., Adams, S., Oberdorf‐Maass, S. U., Behr, B., Vilardaga, J., Tsien, R. Y., Ellisman, M. H., & Lohse, M. J. (2005) · Nature Methods · doi:10.1038/nmeth742 · Cited by 481

The structural basis of agonist-induced activation in constitutively active rhodopsin

Standfuss, J., Edwards, P. C., D’Antona, A. M., Fransen, M. P., Xie, G., Oprian, D. D., & Schertler, G. F. X. (2011) · Nature · doi:10.1038/nature09795 · Cited by 481

Diversity and modularity of G protein-coupled receptor structures

Katritch, V., Cherezov, V., & Stevens, R. C. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.09.003 · Cited by 480

Detection of single fluorescent molecules

Shera, E. B., Seitzinger, N. K., Davis, L. M., Keller, R. A., & Soper, S. A. (1990) · Chemical Physics Letters · doi:10.1016/0009-2614(90)85485-u · Cited by 477

Expanding and Reprogramming the Genetic Code of Cells and Animals

Chin, J. W. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035737 · Cited by 476

Quantitative Assessment of β1- and β2-Adrenergic Receptor Homo- and Heterodimerization by Bioluminescence Resonance Energy Transfer

Mercier, J.-F., Salahpour, A., Angers, S., Breit, A., & Bouvier, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205767200 · Cited by 474

Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor

Bokoch, M. P., Zou, Y., Rasmussen, S. G. F., Liu, C. W., Nygaard, R., Rosenbaum, D. M., Fung, J. J., Choi, H., Thian, F. S., Kobilka, T. S., et al. (2010) · Nature · doi:10.1038/nature08650 · Cited by 473

Bioorthogonal Turn‐On Probes for Imaging Small Molecules inside Living Cells

Devaraj, N. K., Hilderbrand, S. A., Upadhyay, R., Mazitschek, R., & Weissleder, R. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906120 · Cited by 466

Proposed method for molecular optical imaging

Betzig, E. (1995) · Optics Letters · doi:10.1364/ol.20.000237 · Cited by 465

Refined Structure of an Intact IgG2a Monoclonal Antibody ,

Harris, L. J., Larson, S. B., Hasel, K. W., & McPherson, A. (1997) · Biochemistry · doi:10.1021/bi962514+ · Cited by 462

High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P., & Hubbell, W. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802515105 · Cited by 462

Dynamin and β-Arrestin Reveal Distinct Mechanisms for G Protein-coupled Receptor Internalization

Zhang, J., Ferguson, S. S. G., Barak, L. S., Ménard, L., & Caron, M. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18302 · Cited by 459

Structure of the chemokine receptor CXCR1 in phospholipid bilayers

Park, S. H., Das, B. B., Casagrande, F., Tian, Y., Nothnagel, H. J., Chu, M., Kiefer, H., Maier, K., Angelis, A. A. D., Marassi, F. M., et al. (2012) · Nature · doi:10.1038/nature11580 · Cited by 459

Serial Femtosecond Crystallography of G Protein–Coupled Receptors

Liu, W., Wacker, D., Gati, C., Han, G. W., James, D., Wang, D., Nelson, G., Weierstall, U., Katritch, V., Barty, A., et al. (2013) · Science · doi:10.1126/science.1244142 · Cited by 459

Single-molecule analysis of fluorescently labeled G-protein–coupled receptors reveals complexes with distinct dynamics and organization

Calebiro, D., Rieken, F., Wagner, J. A., Sungkaworn, T., Zabel, U., Borzı̀, A., Cocucci, E., Zürn, A., & Lohse, M. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205798110 · Cited by 457

Labeling of fusion proteins with synthetic fluorophores in live cells

Keppler, A., Pick, H. M., Arrivoli, C., Vogel, H., & Johnsson, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401923101 · Cited by 443

The development of cryo-EM into a mainstream structural biology technique

Nogales, E. (2015) · Nature Methods · doi:10.1038/nmeth.3694 · Cited by 441

Introducing genetically encoded aldehydes into proteins

Carrico, I. S., Carlson, B. L., & Bertozzi, C. R. (2007) · Nature Chemical Biology · doi:10.1038/nchembio878 · Cited by 438

New directions in single-molecule imaging and analysis

Moerner, W. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610081104 · Cited by 437

Measurement of the millisecond activation switch of G protein–coupled receptors in living cells

Vilardaga, J., Bünemann, M., Krasel, C., Castro, M., & Lohse, M. J. (2003) · Nature Biotechnology · doi:10.1038/nbt838 · Cited by 432

Probing cellular protein complexes using single-molecule pull-down

Jain, A., Liu, R., Ramani, B., Arauz, E. J., Ishitsuka, Y., Ragunathan, K., Park, J., Chen, J., Xiang, Y. K., & Ha, T. (2011) · Nature · doi:10.1038/nature10016 · Cited by 429

Near-field spectroscopy of single molecules at room temperature

Trautman, J. K., Macklin, J. J., Brus, L. E., & Betzig, E. (1994) · Nature · doi:10.1038/369040a0 · Cited by 428

Amber Suppression: a Nucleotide Change in the Anticodon of a Tyrosine Transfer RNA

Goodman, H. M., Abelson, J. N., Landy, A., Brenner, S., & Smith, J. (1968) · Nature · doi:10.1038/2171019a0 · Cited by 426

Mammalian cell–based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity

Martin, B. R., Giepmans, B. N. G., Adams, S., & Tsien, R. Y. (2005) · Nature Biotechnology · doi:10.1038/nbt1136 · Cited by 424

Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules

Resh, M. D. (2006) · Science s STKE · doi:10.1126/stke.3592006re14 · Cited by 423

Real-time monitoring of receptor and G-protein interactions in living cells

Galès, C., Rebois, R. V., Hogue, M., Trieu, P., Breit, A., Hébert, T. E., & Bouvier, M. (2005) · Nature Methods · doi:10.1038/nmeth743 · Cited by 414

A chemical toolkit for proteins — an expanded genetic code

Xie, J., & Schultz, P. G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2005 · Cited by 408

Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool

Wan, W., Tharp, J. M., & Liu, W. R. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.03.002 · Cited by 398

Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography

Zhang, H., Ünal, H., Gati, C., Han, G. W., Liu, W., Zatsepin, N. A., James, D., Wang, D., Nelson, G., Weierstall, U., et al. (2015) · Cell · doi:10.1016/j.cell.2015.04.011 · Cited by 392

Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes

Molday, R. S., & MacKenzie, D. J. (1983) · Biochemistry · doi:10.1021/bi00272a020 · Cited by 391

Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase

Diez, M., Zimmermann, B., Börsch, M., König, M., Schweinberger, E., Steigmiller, S., Reuter, R., Felekyan, S., Kudryavtsev, V., Seidel, C. A. M., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb718 · Cited by 391

Biocompatible Copper(I) Catalysts for in Vivo Imaging of Glycans

del Amo, D. S., Wang, W., Jiang, H., Besanceney, C., Yan, A. C., Levy, M., Liu, Y., Marlow, F. L., & Wu, P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja106553e · Cited by 390

Zur Existenz niedergliedriger Cycloalkine, I

Wittig, G., & Krebs, A. W. (1961) · Chemische Berichte · doi:10.1002/cber.19610941213 · Cited by 388

Adding Amino Acids with Novel Reactivity to the Genetic Code of Saccharomyces Cerevisiae

Deiters, A., Cropp, T. A., Mukherji, M., Chin, J. W., Anderson, J. C., & Schultz, P. G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0370037 · Cited by 386

Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F

Sheikh, S. P., Zvyaga, T. A., Lichtarge, O., Sakmar, T. P., & Bourne, H. R. (1996) · Nature · doi:10.1038/383347a0 · Cited by 385

Probing Protein Electrostatics with a Synthetic Fluorescent Amino Acid

Cohen, B. E., McAnaney, T. B., Park, E. S., Jan, Y. N., Boxer, S. G., & Jan, L. Y. (2002) · Science · doi:10.1126/science.1069346 · Cited by 382

Formation and dissociation of M 1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules

Hern, J. A., Baig, A. H., Mashanov, G. I., Birdsall, B., Corrie, J. E. T., Lazareno, S., Molloy, J. E., & Birdsall, N. J. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907915107 · Cited by 381

Structure and Function in Rhodopsin

Farrens, D., & Khorana, H. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5073 · Cited by 381

Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes

Fernández-Suárez, M., Baruah, H., Martínez-Hernández, L., Xie, K. T., Baskin, J. M., Bertozzi, C. R., & Ting, A. Y. (2007) · Nature Biotechnology · doi:10.1038/nbt1355 · Cited by 376

Native Chemical Ligation and Extended Methods: Mechanisms, Catalysis, Scope, and Limitations

Agouridas, V., Mahdi, O. E., Diemer, V., Cargoët, M., Monbaliu, J. M., & Melnyk, O. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00712 · Cited by 656

Common activation mechanism of class A GPCRs

Zhou, Q., Yang, D., Wu, M., Guo, Y., Guo, W., Li, Z., Cai, X., Dai, A., Jang, W., Shakhnovich, E. I., et al. (2019) · eLife · doi:10.7554/elife.50279 · Cited by 648

Molecular Imprinting: Materials Nanoarchitectonics with Molecular Information

Komiyama, M., Mori, T., & Ariga, K. (2018) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20180084 · Cited by 231

Conducting Nanomaterial Sensor Using Natural Receptors

Kwon, O. S., Song, H. S., Park, T. H., & Jang, J. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00159 · Cited by 226

Super-Resolution Microscopy: Shedding Light on the Cellular Plasma Membrane

Stone, M. B., Shelby, S. A., & Veatch, S. L. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00716 · Cited by 168

Exploring GPCR conformational dynamics using single-molecule fluorescence

Agyemang, E., Gonneville, A. N., Krishnan, S. T., & Lamichhane, R. (2024) · Methods · doi:10.1016/j.ymeth.2024.03.011 · Cited by 12

G Protein–Coupled Receptor Pharmacology at the Single-Molecule Level

Calebiro, D., & Grimes, J. (2019) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010919-023348 · Cited by 27

Progress of single-molecule detection of G protein-coupled receptor activation

Zhang, Y. (2008) · Shengming kexue

Single-Molecule Imaging of GPCR Interactions

Calebiro, D., & Sungkaworn, T. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.10.010 · Cited by 74

Toward Fluorescent Probes for G‑Protein-Coupled Receptors (GPCRs)

Ma, Z., Du, L., & Li, M. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401823z · Cited by 62