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

Agonists induce conformational changes in transmembrane domains III and VI of the β2 adrenoceptor

Gether, U., Lin, S., Ghanouni, P., Ballesteros, J. A., Weinstein, H., & Kobilka, B. K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.22.6737 · Cited by 375

Genetic incorporation of unnatural amino acids into proteins in mammalian cells

Liu, W. R., Brock, A., Chen, S., Chen, S., & Schultz, P. G. (2007) · Nature Methods · doi:10.1038/nmeth1016 · Cited by 374

Ligand-directed tosyl chemistry for protein labeling in vivo

Tsukiji, S., Miyagawa, M., Takaoka, Y., Tamura, T., & Hamachi, I. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.157 · Cited by 373

Functionally Different Agonists Induce Distinct Conformations in the G Protein Coupling Domain of the β2Adrenergic Receptor

Ghanouni, P., Gryczynski, Z. K., Steenhuis, J. J., Lee, T. W., Farrens, D., Lakowicz, J. R., & Kobilka, B. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100162200 · Cited by 364

A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency

Schmidt, B., Selmer, T., Ingendoh, A., & von Figurat, K. (1995) · Cell · doi:10.1016/0092-8674(95)90314-3 · Cited by 361

Alternating-Laser Excitation of Single Molecules

Kapanidis, A. N., Laurence, T. A., Lee, N. K., Margeat, E., Kong, X., & Weiss, S. (2005) · Accounts of Chemical Research · doi:10.1021/ar0401348 · Cited by 359

Fluorescence spectroscopy and spectral diffusion of single impurity molecules in a crystal

Ambrose, W. P., & Moerner, W. E. (1991) · Nature · doi:10.1038/349225a0 · Cited by 358

Interaction of Chemokine Receptor CCR5 with its Ligands: Multiple Domains for HIV-1 gp120 Binding and a Single Domain for Chemokine Binding

Wu, L., LaRosa, G. J., Kassam, N., Gordon, C. J., Heath, H., Ruffing, N., Chen, H., Humblias, J., Samson, M., Parmentier, M., et al. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.8.1373 · Cited by 357

Real-time tRNA transit on single translating ribosomes at codon resolution

Uemura, S., Aitken, C. E., Korlach, J., Flusberg, B. A., Turner, S. W., & Puglisi, J. D. (2010) · Nature · doi:10.1038/nature08925 · Cited by 356

Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking

Hubbell, W. L., Altenbach, C., Hubbell, C., & Khorana, H. G. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)63010-x · Cited by 353

Coupling ligand structure to specific conformational switches in the β2-adrenoceptor

Yao, X.-J., Parnot, C., Deupí, X., Ratnala, V. R. P., Swaminath, G., Farrens, D., & Kobilka, B. K. (2006) · Nature Chemical Biology · doi:10.1038/nchembio801 · Cited by 353

Activation of the A2A adenosine G-protein-coupled receptor by conformational selection

Ye, L., Eps, N. V., Zimmer, M., Ernst, O. P., & Prosser, R. S. (2016) · Nature · doi:10.1038/nature17668 · Cited by 353

Full characterization of GPCR monomer–dimer dynamic equilibrium by single molecule imaging

Kasai, R. S., Suzuki, K. G. N., Prossnitz, E. R., Koyama‐Honda, I., Nakada, C., Fujiwara, T. K., & Kusumi, A. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009128 · Cited by 349

Amino Acids for Diels–Alder Reactions in Living Cells

Plass, T., Milles, S., Koehler, C., Szymański, J., Mueller, R., Wießler, M., Schultz, C., & Lemke, E. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201108231 · Cited by 347

Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions

Guimarães, C. P., Witte, M. D., Theile, C. S., Bozkurt, G., Kundrat, L., Blom, A. E. M., & Ploegh, H. L. (2013) · Nature Protocols · doi:10.1038/nprot.2013.101 · Cited by 346

Time-resolved FRET between GPCR ligands reveals oligomers in native tissues

Albizu, L., Cottet, M., Králíková, M., Stoev, S. B., Seyer, R., Brabet, I., Roux, T., Bazin, H., Bourrier, E., Lamarque, L., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.396 · Cited by 340

Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time

Churchman, L. S., Ökten, Z., Rock, R. S., Dawson, J., & Spudich, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409487102 · Cited by 338

G protein‐coupled receptor hetero‐dimerization: contribution to pharmacology and function

Milligan, G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00169.x · Cited by 335

BODIPY–Tetrazine Derivatives as Superbright Bioorthogonal Turn‐on Probes

Carlson, J., Meimetis, L. G., Hilderbrand, S. A., & Weissleder, R. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201301100 · Cited by 334

Sequential Binding of Agonists to the β2 Adrenoceptor

Swaminath, G., Xiang, Y. K., Lee, T. W., Steenhuis, J. J., Parnot, C., & Kobilka, B. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310888200 · Cited by 333

Apo-Ghrelin Receptor Forms Heteromers with DRD2 in Hypothalamic Neurons and Is Essential for Anorexigenic Effects of DRD2 Agonism

Kern, A., Albarran-Zeckler, R. G., Walsh, H. E., & Smith, R. G. (2012) · Neuron · doi:10.1016/j.neuron.2011.10.038 · Cited by 330

Fluorescence Imaging with One Nanometer Accuracy: Application to Molecular Motors

Yıldız, A., & Selvin, P. R. (2005) · Accounts of Chemical Research · doi:10.1021/ar040136s · Cited by 328

In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag

Miller, L. W., Cai, Y., Sheetz, M. P., & Cornish, V. W. (2005) · Nature Methods · doi:10.1038/nmeth749 · Cited by 327

A new approach to analyze cell surface protein complexes reveals specific heterodimeric metabotropic glutamate receptors

Doumazane, E., Scholler, P., Zwier, J. M., Trinquet, E., Rondard, P., & Pin, J. (2011) · The FASEB Journal · doi:10.1096/fj.10-163147 · Cited by 324

The GPCR Network: a large-scale collaboration to determine human GPCR structure and function

Stevens, R. C., Cherezov, V., Katritch, V., Abagyan, R. A., Kühn, P., Rosen, H., & Wüthrich, K. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3859 · Cited by 324

Genetically Encoded Copper‐Free Click Chemistry

Plass, T., Milles, S., Koehler, C., Schultz, C., & Lemke, E. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201008178 · Cited by 324

A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer

James, J. R., Oliveira, M. I., Carmo, A. M., Iaboni, A., & Davis, S. J. (2006) · Nature Methods · doi:10.1038/nmeth978 · Cited by 320

Antagonism of dopamine D2 receptor/β-arrestin 2 interaction is a common property of clinically effective antipsychotics

Masri, B., Salahpour, A., Didriksen, M., Ghisi, V., Beaulieu, J., Gainetdinov, R. R., & Caron, M. G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803522105 · Cited by 320

A Genetically Encoded Fluorescent Amino Acid

Wang, J., Xie, J., & Schultz, P. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062666k · Cited by 319

G-protein-coupled receptors function as oligomers in vivo

Overton, M. C., & BLUMER, K. J. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00386-9 · Cited by 318

Genetic Encoding and Labeling of Aliphatic Azides and Alkynes in Recombinant Proteins via a Pyrrolysyl-tRNA Synthetase/tRNA CUA Pair and Click Chemistry

Nguyen, D., Lusic, H., Neumann, H., Kapadnis, P. B., Deiters, A., & Chin, J. W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900553w · Cited by 318

Fluorescence/Bioluminescence Resonance Energy Transfer Techniques to Study G-Protein-Coupled Receptor Activation and Signaling

Lohse, M. J., Nuber, S., & Hoffmann, C. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004309 · Cited by 318

Inter- and Intramolecular Fluorescence Quenching of Organic Dyes by Tryptophan

Marmé, N., Knemeyer, J., Sauer, M., & Wolfrum, J. (2003) · Bioconjugate Chemistry · doi:10.1021/bc0341324 · Cited by 313

Directed Evolution of O6-Alkylguanine-DNA Alkyltransferase for Efficient Labeling of Fusion Proteins with Small Molecules In Vivo

Juillerat, A., Gronemeyer, T., Keppler, A., Gendreizig, S., Pick, H. M., Vogel, H., & Johnsson, K. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00068-1 · Cited by 313

Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.

Karnik, S. S., & Khorana, H. G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38195-x · Cited by 310

Fluorogenic click reaction

Droumaguet, C. L., Wang, C., & Wang, Q. (2009) · Chemical Society Reviews · doi:10.1039/b901975h · Cited by 306

A Brief History of G‐Protein Coupled Receptors (Nobel Lecture)

Lefkowitz, R. J. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201301924 · Cited by 306

Segregation of molecules at cell division reveals native protein localization

Landgraf, D., Okumuş, B., Chien, P., Baker, T. A., & Paulsson, J. (2012) · Nature Methods · doi:10.1038/nmeth.1955 · Cited by 301

Preventing Thiol-Yne Addition Improves the Specificity of Strain-Promoted Azide–Alkyne Cycloaddition

van Geel, R., Pruijn, G. J. M., van Delft, F. L., & Boelens, W. C. (2012) · Bioconjugate Chemistry · doi:10.1021/bc200365k · Cited by 299

Recent developments in biased agonism

Wisler, J. W., Xiao, K., Thomsen, A. R. B., & Lefkowitz, R. J. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.10.008 · Cited by 297

Homodimerization of the β2-Adrenergic Receptor as a Prerequisite for Cell Surface Targeting

Salahpour, A., Angers, S., Mercier, J.-F., Lagacé, M., Marullo, S., & Bouvier, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403363200 · Cited by 297

A fluorophore ligase for site-specific protein labeling inside living cells

Uttamapinant, C., White, K. A., Baruah, H., Thompson, S., Fernández-Suárez, M., Puthenveetil, S., & Ting, A. Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914067107 · Cited by 295

Curvature and Hydrophobic Forces Drive Oligomerization and Modulate Activity of Rhodopsin in Membranes

Botelho, A. V., Huber, T., Sakmar, T. P., & Brown, M. F. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.082776 · Cited by 292

A Versatile Platform for Single- and Multiple-Unnatural Amino Acid Mutagenesis in Escherichia coli

Chatterjee, A., Sun, S. B., Furman, J. L., Xiao, H., & Schultz, P. G. (2013) · Biochemistry · doi:10.1021/bi4000244 · Cited by 285

Fluorescent Labeling of Purified β2 Adrenergic Receptor

Gether, U., Lin, S., & Kobilka, B. K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28268 · Cited by 280

Structural basis for nucleotide exchange in heterotrimeric G proteins

Dror, R. O., Mildorf, T. J., Hilger, D., Manglik, A., Borhani, D. W., Arlow, D. H., Philippsen, A., Villanueva, N., Yang, Z., Lerch, M. T., et al. (2015) · Science · doi:10.1126/science.aaa5264 · Cited by 280

Adding l-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-tRNA synthetases

Mukai, T., Kobayashi, T., Hino, N., Yanagisawa, T., Sakamoto, K., & Yokoyama, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.164 · Cited by 279

Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells

Sakamoto, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf589 · Cited by 276

A genetically encoded fluorescent amino acid

Summerer, D., Chen, S., Wu, N., Deiters, A., Chin, J. W., & Schultz, P. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603965103 · Cited by 274

Site-specific N-terminal labeling of proteins using sortase-mediated reactions

Theile, C. S., Witte, M. D., Blom, A. E. M., Kundrat, L., Ploegh, H. L., & Guimarães, C. P. (2013) · Nature Protocols · doi:10.1038/nprot.2013.102 · Cited by 274

Efficient Multisite Unnatural Amino Acid Incorporation in Mammalian Cells via Optimized Pyrrolysyl tRNA Synthetase/tRNA Expression and Engineered eRF1

Schmied, W. H., Elsässer, S. J., Uttamapinant, C., & Chin, J. W. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5069728 · Cited by 272

Energy Landscapes as a Tool to Integrate GPCR Structure, Dynamics, and Function

Deupí, X., & Kobilka, B. K. (2010) · Physiology · doi:10.1152/physiol.00002.2010 · Cited by 272

Efficiency of blocking of non-specific interaction of different proteins by BSA adsorbed on hydrophobic and hydrophilic surfaces

Jeyachandran, Y. L., Mielczarski, J. A., Mielczarski, E., & Rai, B. (2009) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2009.09.007 · Cited by 271

Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors

Fotiadis, D., Jastrzębska, B., Philippsen, A., Müller, D. J., Palczewski, K., & Engel, A. H. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.03.013 · Cited by 271

Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRET

Wang, K., Sachdeva, A., Cox, D. J., Wilf, N. M., Lang, K., Wallace, S., Mehl, R. A., & Chin, J. W. (2014) · Nature Chemistry · doi:10.1038/nchem.1919 · Cited by 270

A Facile System for Encoding Unnatural Amino Acids in Mammalian Cells

Chen, P. R., Groff, D., Guo, J., Ou, W., Cellitti, S. E., Geierstanger, B. H., & Schultz, P. G. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900683 · Cited by 270

Efficient Coupling of Transducin to Monomeric Rhodopsin in a Phospholipid Bilayer

Whorton, M. R., Jastrzębska, B., Park, P. S. ‐., Fotiadis, D., Engel, A. H., Palczewski, K., & Sunahara, R. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703346200 · Cited by 269

Rapid Hop Diffusion of a G-Protein-Coupled Receptor in the Plasma Membrane as Revealed by Single-Molecule Techniques

Suzuki, K. G. N., Ritchie, K. P., Kajikawa, E., Fujiwara, T. K., & Kusumi, A. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.048538 · Cited by 269

Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging

Gahlmann, A., & Moerner, W. E. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro3154 · Cited by 268

Development of SNAP‐Tag Fluorogenic Probes for Wash‐Free Fluorescence Imaging

Sun, X., Zhang, A., Baker, B., Sun, L., Howard, A., Buswell, J., Maurel, D., Masharina, A., Johnsson, K., Noren, C. J., et al. (2011) · ChemBioChem · doi:10.1002/cbic.201100173 · Cited by 267

Tracking G-protein-coupled receptor activation using genetically encoded infrared probes

Ye, S., Zaitseva, E., Caltabiano, G., Schertler, G. F. X., Sakmar, T. P., Deupí, X., & Vogel, R. (2010) · Nature · doi:10.1038/nature08948 · Cited by 266

A Genetically Encoded Infrared Probe

Schultz, K. C., Supeková, Ľ., Ryu, Y., Xie, J., Perera, R., & Schultz, P. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0636690 · Cited by 265

Direct charging of tRNACUA with pyrrolysine in vitro and in vivo

Blight, S. K., Larue, R. C., Mahapatra, A., Longstaff, D. G., Chang, E. S., Zhao, G., Kang, P. T., Green‐Church, K. B., Chan, M. K., & Krzycki, J. A. (2004) · Nature · doi:10.1038/nature02895 · Cited by 265

Conformational cross-talk between α2A-adrenergic and μ-opioid receptors controls cell signaling

Vilardaga, J., Nikolaev, V. O., Lorenz, K., Ferrandon, S., Zhuang, Z., & Lohse, M. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.64 · Cited by 264

Palladium-Mediated Cell-Surface Labeling

Spicer, C. D., Triemer, T., & Davis, B. G. (2011) · Journal of the American Chemical Society · doi:10.1021/ja209352s · Cited by 264

Quantitative Photo Activated Localization Microscopy: Unraveling the Effects of Photoblinking

Annibale, P., Vanni, S., Scarselli, M., Röthlisberger, U., & Rađenović, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022678 · Cited by 262

Agonist-induced Destabilization of β-Adrenergic Receptor mRNA

Hadcock, J. R., Wang, H. Y., & Malbon, C. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47200-1 · Cited by 260

Ultrafluorogenic Coumarin–Tetrazine Probes for Real‐Time Biological Imaging

Meimetis, L. G., Carlson, J., Giedt, R. J., Köhler, R. H., & Weissleder, R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403890 · Cited by 259

Surface Passivation for Single-molecule Protein Studies

Chandradoss, S. D., Haagsma, A. C., Lee, Y. K., Hwang, J., Nam, J., & Joo, C. (2014) · Journal of Visualized Experiments · doi:10.3791/50549 · Cited by 258

Monitoring Receptor Oligomerization Using Time-resolved Fluorescence Resonance Energy Transfer and Bioluminescence Resonance Energy Transfer

McVey, M., Ramsay, D., Kellett, E., Rees, S., Wilson, S., Pope, A. J., & Milligan, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008902200 · Cited by 257

Probing the β2 Adrenoceptor Binding Site with Catechol Reveals Differences in Binding and Activation by Agonists and Partial Agonists

Swaminath, G., Deupí, X., Lee, T. W., Zhu, W., Thian, F. S., Kobilka, T. S., & Kobilka, B. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502352200 · Cited by 257

Structural Features and Light-Dependent Changes in the Cytoplasmic Interhelical E−F Loop Region of Rhodopsin: A Site-Directed Spin-Labeling Study

Altenbach, C., Yang, K., Farrens, D., Farahbakhsh, Z. T., Khorana, H. G., & Hubbell, W. L. (1996) · Biochemistry · doi:10.1021/bi960849l · Cited by 256

Expanding the Genetic Code of an Animal

Greiss, S., & Chin, J. W. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2054034 · Cited by 254

Multiple ligand-specific conformations of the β2-adrenergic receptor

Kahsai, A. W., Xiao, K., Rajagopal, S., Ahn, S., Shukla, A. K., Sun, J., Oas, T. G., & Lefkowitz, R. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.634 · Cited by 252

Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin

Howarth, M. R., & Ting, A. Y. (2008) · Nature Protocols · doi:10.1038/nprot.2008.20 · Cited by 249

Conformational transitions in DNA polymerase I revealed by single-molecule FRET

Santoso, Y., Joyce, C. M., Potapova, O., Reste, L. L., Hohlbein, J., Torella, J. P., Grindley, N. D. F., & Kapanidis, A. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910909107 · Cited by 248

Site-specific chemical protein conjugation using genetically encoded aldehyde tags

Rabuka, D., Rush, J. S., deHart, G. W., Wu, P., & Bertozzi, C. R. (2012) · Nature Protocols · doi:10.1038/nprot.2012.045 · Cited by 247

Incorporation of Nonnatural Amino Acids Into Proteins

Hendrickson, T. L., de Crécy‐Lagard, V., & SCHIMMEL, P. R. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.012803.092429 · Cited by 245

The role of protein dynamics in GPCR function: insights from the β2AR and rhodopsin

Manglik, A., & Kobilka, B. K. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.01.008 · Cited by 244

Site-specific incorporation of biophysical probes into proteins.

Cornish, V. W., Benson, D. R., Altenbach, C., Hideg, K., Hubbell, W. L., & Schultz, P. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.2910 · Cited by 243

Unnatural amino acids as probes of protein structure and function

Dougherty, D. D. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00148-4 · Cited by 243

Suppressing Brownian motion of individual biomolecules in solution

Cohen, A. E., & Moerner, W. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509976103 · Cited by 242

Enzymatic Labeling of Proteins: Techniques and Approaches

Rashidian, M., Dozier, J. K., & Distefano, M. D. (2013) · Bioconjugate Chemistry · doi:10.1021/bc400102w · Cited by 242

Azide: A Unique Dipole for Metal‐Free Bioorthogonal Ligations

Debets, M. F., van der Doelen, C. W. J., Rutjes, F. P. J. T., & van Delft, F. L. (2010) · ChemBioChem · doi:10.1002/cbic.201000064 · Cited by 240

Dynamic Distribution of Chemoattractant Receptors in Living Cells During Chemotaxis and Persistent Stimulation

Xiao, Z., Zhang, N., Murphy, D. B., & Devreotes, P. N. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.365 · Cited by 236

Nanobody stabilization of G protein-coupled receptor conformational states

Steyaert, J., & Kobilka, B. K. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.06.011 · Cited by 234

A Genetically Encoded Fluorescent Probe in Mammalian Cells

Chatterjee, A., Guo, J., Lee, H. S., & Schultz, P. G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4059553 · Cited by 234

Nicotinic Receptor Binding Site Probed with Unnatural Amino Acid Incorporation in Intact Cells

Nowak, M. W., Kearney, P. C., Sampson, Saks, M. E., Labarca, C. G., Silverman, S. K., Zhong, W., Thorson, J. S., Abelson, J. N., Davidson, N., et al. (1995) · Science · doi:10.1126/science.7716551 · Cited by 230

Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

Westfield, G., Rasmussen, S. G. F., Su, M., Dutta, S., DeVree, B. T., Chung, K. Y., Calinski, D. M., Vélez-Ruiz, G. A., Oleskie, A. N., Pardon, E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113645108 · Cited by 230

Distinct conformational changes in β-arrestin report biased agonism at seven-transmembrane receptors

Shukla, A. K., Violin, J. D., Whalen, E. J., Gesty‐Palmer, D., Shenoy, S. K., & Lefkowitz, R. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804246105 · Cited by 230

Stereospecific [3H](−)-alprenolol binding sites, β-adrenergic receptors and adenylate cyclase

Lefkowitz, R. J., Mukherjee, C., Coverstone, M., & Caron, M. G. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90297-6 · Cited by 229

Genetic Incorporation of a Small, Environmentally Sensitive, Fluorescent Probe into Proteins in Saccharomyces cerevisiae

Lee, H. S., Guo, J., Lemke, E. A., Dimla, R. D., & Schultz, P. G. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904896s · Cited by 226

Imaging Three-Dimensional Single Molecule Orientations

Bartko, A. P., & Dickson, R. M. (1999) · The Journal of Physical Chemistry B · doi:10.1021/jp993364q · Cited by 226

A general approach for the generation of orthogonal tRNAs

Wang, L., & Schultz, P. G. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00063-1 · Cited by 226

Protein induced fluorescence enhancement (PIFE) for probing protein–nucleic acid interactions

Hwang, H. H., & Myong, S. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60201j · Cited by 222

Expanding the Genetic Code of Yeast for Incorporation of Diverse Unnatural Amino Acids via a Pyrrolysyl-tRNA Synthetase/tRNA Pair

Hancock, S. M., Uprety, R., Deiters, A., & Chin, J. W. (2010) · Journal of the American Chemical Society · doi:10.1021/ja104609m · Cited by 220

Endosomal generation of cAMP in GPCR signaling

Vilardaga, J., Jean‐Alphonse, F., & Gardella, T. J. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1611 · Cited by 219

GPCR monomers and oligomers: it takes all kinds

Gurevich, V. V., & Gurevich, E. V. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2007.11.007 · Cited by 219

Breaking the concentration limit of optical single-molecule detection

Holzmeister, P., Acuna, G. P., Grohmann, D., & Tinnefeld, P. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60207a · Cited by 219

Internal Trafficking and Surface Mobility of a Functionally Intact β2-Adrenergic Receptor-Green Fluorescent Protein Conjugate

Barak, L. S., Ferguson, S. S. G., Zhang, J., Martenson, C. H., Meyer, T., & Caron, M. G. (1997) · Molecular Pharmacology · doi:10.1124/mol.51.2.177 · Cited by 219

The conformational signature of β-arrestin2 predicts its trafficking and signalling functions

Lee, M., Appleton, K. M., Strungs, E. G., Kwon, J. Y., Morinelli, T. A., Peterson, Y. K., Laporte, S. A., & Luttrell, L. M. (2016) · Nature · doi:10.1038/nature17154 · Cited by 219

Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit

Ernst, O. P., Gramse, V., Kolbe, M., Hofmann, K. P., & Heck, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701967104 · Cited by 216

Fluorescent labeling of tetracysteine-tagged proteins in intact cells

Hoffmann, C., Gaietta, G. M., Zürn, A., Adams, S., Terrillon, S., Ellisman, M. H., Tsien, R. Y., & Lohse, M. J. (2010) · Nature Protocols · doi:10.1038/nprot.2010.129 · Cited by 215

Genetically Encoded Cyclopropene Directs Rapid, Photoclick‐Chemistry‐Mediated Protein Labeling in Mammalian Cells

Yu, Z., Pan, Y., Wang, Z., Wang, J., & Lin, Q. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201205352 · Cited by 214

Methods to monitor the quaternary structure of G protein‐coupled receptors

Milligan, G., & Bouvier, M. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04731.x · Cited by 213

A Facile System for Genetic Incorporation of Two Different Noncanonical Amino Acids into One Protein in Escherichia coli

Wan, W., Huang, Y. R., Wang, Z., Russell, W. K., Pai, P., Russell, D. H., & Liu, W. R. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000465 · Cited by 213

A general and efficient route for chemical aminoacylation of transfer RNAs

Robertson, S. A., Ellman, J. A., & Schultz, P. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00007a055 · Cited by 211

Site-Specific Incorporation of a 19F-Amino Acid into Proteins as an NMR Probe for Characterizing Protein Structure and Reactivity

Jackson, J. C., Hammill, J. T., & Mehl, R. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja064661t · Cited by 211

Analysis of receptor oligomerization by FRAP microscopy

Dorsch, S., Klotz, K., Engelhardt, S. H., Lohse, M. J., & Bünemann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1304 · Cited by 211

Ligand-Directed Acyl Imidazole Chemistry for Labeling of Membrane-Bound Proteins on Live Cells

Fujishima, S., Yasui, R., Miki, T., Ojida, A., & Hamachi, I. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2108855 · Cited by 210

Constitutive Agonist-independent CCR5 Oligomerization and Antibody-mediated Clustering Occurring at Physiological Levels of Receptors

Issafras, H., Angers, S., Bulenger, S., Blanpain, C., Parmentier, M., Labbé‐Jullié, C., Bouvier, M., & Marullo, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202386200 · Cited by 209

THE ROLE OF SULFHYDRYL GROUPS IN THE BLEACHING AND SYNTHESIS OF RHODOPSIN

Wald, G., & Brown, P. K. (1952) · The Journal of General Physiology · doi:10.1085/jgp.35.5.797 · Cited by 208

Imaging bacterial peptidoglycan with near-infrared fluorogenic azide probes

Shieh, P., Siegrist, M. S., Cullen, A. J., & Bertozzi, C. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322727111 · Cited by 207

Membrane Trafficking of G Protein–Coupled Receptors

Tan, C. M., Brady, A. E., Nickols, H. H., Wang, Q., & Limbird, L. E. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121558 · Cited by 207

β-Arrestin biosensors reveal a rapid, receptor-dependent activation/deactivation cycle

Nuber, S., Zabel, U., Lorenz, K., Nuber, A., Milligan, G., Tobin, A. B., Lohse, M. J., & Hoffmann, C. (2016) · Nature · doi:10.1038/nature17198 · Cited by 207

Confined Diffusion Without Fences of a G-Protein-Coupled Receptor as Revealed by Single Particle Tracking

Daumas, F., Destainville, N., Millot, C., Lopez, A., Dean, D. S., & Salomé, L. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74856-5 · Cited by 203

In Situ Synthesis of Alkenyl Tetrazines for Highly Fluorogenic Bioorthogonal Live‐Cell Imaging Probes

Wu, H., Yang, J., Šečkutė, J., & Devaraj, N. K. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201400135 · Cited by 202

Expanding the genetic code of Drosophila melanogaster

Bianco, A., Townsley, F. M., Greiss, S., Lang, K., & Chin, J. W. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1043 · Cited by 198

An aminoacyl-tRNA synthetase that specifically activates pyrrolysine

Polycarpo, C. R., Ambrogelly, A., Bérubé, A., Winbush, S. M., McCloskey, J. A., Crain, P. F., Wood, J. L., & Söll, D. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405362101 · Cited by 195

Progress toward the evolution of an organism with an expanded genetic code

Liu, D. R., & Schultz, P. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4780 · Cited by 193

Single Molecules, Cells, and Super‐Resolution Optics (Nobel Lecture)

Betzig, E. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201501003 · Cited by 192

FTIR analysis of GPCR activation using azido probes

Ye, S., Huber, T., Vogel, R., & Sakmar, T. P. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.167 · Cited by 191

Coordinate-based colocalization analysis of single-molecule localization microscopy data

Malkusch, S., Endesfelder, U., Mondry, J., Gelléri, M., Verveer, P. J., & Heilemann, M. (2011) · Histochemistry and Cell Biology · doi:10.1007/s00418-011-0880-5 · Cited by 191

Constitutive and Agonist-dependent Homo-oligomerization of the Thyrotropin-releasing Hormone Receptor

Kroeger, K. M., Hanyaloglu, A. C., Seeber, R. M., Miles, L. E. C., & Eidne, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011311200 · Cited by 190

Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells

Patel, R. C., Kumar, U., Lamb, D. C., Eid, J. S., Rocheville, M., Grant, M. P., Rani, A., Hazlett, T. L., Patel, S. C., Gratton, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042705099 · Cited by 190

Proximity Relationships in Rhodopsin

Wu, C., & Stryer, L. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.5.1104 · Cited by 189

The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli

Bose, M., Groff, D., Xie, J., Brustad, E. M., & Schultz, P. G. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055467u · Cited by 188

Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality

Nozawa, K., O’Donoghue, P., Gundllapalli, S. B., Araiso, Y., Ishitani, R., Umehara, T., Söll, D. G., & Nureki, O. (2008) · Nature · doi:10.1038/nature07611 · Cited by 185

Selective Recognition of Protein Tetraserine Motifs with a Cell-Permeable, Pro-fluorescent Bis-boronic Acid

Halo, T. L., Appelbaum, J., Hobert, E. M., Balkin, D. M., & Schepartz, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja807872s · Cited by 185

Ligand‐regulated oligomerization of β2‐adrenoceptors in a model lipid bilayer

Fung, J. J., Deupí, X., Pardo, L., Xiao, Y., Vélez-Ruiz, G. A., DeVree, B. T., Sunahara, R. K., & Kobilka, B. K. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.267 · Cited by 183

High-Throughput Screening of G Protein-Coupled Receptor Antagonists Using a Bioluminescence Resonance Energy Transfer 1-Based β-Arrestin2 Recruitment Assay

Hamdan, F. F., Audet, M., Garneau, P., Pelletier, J., & Bouvier, M. (2005) · SLAS Discovery · doi:10.1177/1087057105275344 · Cited by 183

Site-Specific Protein Modification Using a Ketone Handle

Cornish, V. W., Hahn, K. M., & Schultz, P. G. (1996) · Journal of the American Chemical Society · doi:10.1021/ja961216x · Cited by 182

The Structural Basis of G‐Protein‐Coupled Receptor Signaling (Nobel Lecture)

Kobilka, B. K. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201302116 · Cited by 182

Reaction Rates and Mechanisms for Radical, Photoinitated Addition of Thiols to Alkynes, and Implications for Thiol−Yne Photopolymerizations and Click Reactions

Fairbanks, B. D., Sims, E. A., Anseth, K. S., & Bowman, C. N. (2010) · Macromolecules · doi:10.1021/ma1002968 · Cited by 181

Labeling proteins on live mammalian cells using click chemistry

Nikić, I., Kang, J. H., Girona, G. E., Aramburu, I. V., & Lemke, E. A. (2015) · Nature Protocols · doi:10.1038/nprot.2015.045 · Cited by 181

A Close Look at Fluorescence Quenching of Organic Dyes by Tryptophan

Doose, S., Neuweiler, H., & Sauer, M. (2005) · ChemPhysChem · doi:10.1002/cphc.200500191 · Cited by 180

Genetic Encoding of a Bicyclo[6.1.0]nonyne‐Charged Amino Acid Enables Fast Cellular Protein Imaging by Metal‐Free Ligation

Borrmann, A., Milles, S., Plass, T., Dommerholt, J., Verkade, J. M. M., Wießler, M., Schultz, C., van Hest, J. C. M., van Delft, F. L., & Lemke, E. A. (2012) · ChemBioChem · doi:10.1002/cbic.201200407 · Cited by 180

Genetically encoding unnatural amino acids for cellular and neuronal studies

Wang, W., Takimoto, J. K., Louie, G. V., Baiga, T. J., Noel, J. P., Lee, K., Slesinger, P. A., & Wang, L. (2007) · Nature Neuroscience · doi:10.1038/nn1932 · Cited by 179

Lanthanide Complex-Based Fluorescence Label for Time-Resolved Fluorescence Bioassay

Yuan, J., & Wang, G. (2005) · Journal of Fluorescence · doi:10.1007/s10895-005-2829-3 · Cited by 179

Multiscale Spatial Organization of RNA Polymerase in Escherichia coli

Endesfelder, U., Finan, K., Holden, S. J., Cook, P. R., Kapanidis, A. N., & Heilemann, M. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.05.048 · Cited by 178

Therapeutic antibodies directed at G protein-coupled receptors

Hutchings, C. J., Koglin, M., & Marshall, F. H. (2010) · mAbs · doi:10.4161/mabs.2.6.13420 · Cited by 176

FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids

Kajihara, D., Abe, R., Iijima, I., Komiyama, C., Sisido, M., & Hohsaka, T. (2006) · Nature Methods · doi:10.1038/nmeth945 · Cited by 176

Visualization of G Protein-coupled Receptor Trafficking with the Aid of the Green Fluorescent Protein

Tarasova, N. I., Stauber, R. H., Choi, J. K., Hudson, E. A., Czerwinski, G., Miller, J. L., Pavlakis, G. N., Michejda, C. J., & Wank, S. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14817 · Cited by 176

Use of peptide tagging to detect proteins expressed from cloned genes: deletion mapping functional domains of Drosophila hsp 70.

Munro, S., & Pelham, H. R. B. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02263.x · Cited by 175

Receptor Activation and Homer Differentially Control the Lateral Mobility of Metabotropic Glutamate Receptor 5 in the Neuronal Membrane

Sergé, A., Fourgeaud, L., Hémar, A., & Choquet, D. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-10-03910.2002 · Cited by 175

Genetically Encoded 1,2-Aminothiols Facilitate Rapid and Site-Specific Protein Labeling via a Bio-orthogonal Cyanobenzothiazole Condensation

Nguyen, D., Elliott, T., Holt, M. T., Muir, T. W., & Chin, J. W. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203111c · Cited by 175

Purification and Functional Reconstitution of Monomeric μ-Opioid Receptors

Kuszak, A. J., Pitchiaya, S., Anand, J. P., Mosberg, H. I., Walter, N. G., & Sunahara, R. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026922 · Cited by 175

Genetically Encoded Chemical Probes in Cells Reveal the Binding Path of Urocortin-I to CRF Class B GPCR

Coin, I., Katritch, V., Sun, T., Xiang, Z., Siu, F., Beyermann, M., Stevens, R. C., & Wang, L. (2013) · Cell · doi:10.1016/j.cell.2013.11.008 · Cited by 175

Monitoring agonist‐promoted conformational changes of β‐arrestin in living cells by intramolecular BRET

Charest, P. G., Terrillon, S., & Bouvier, M. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400373 · Cited by 172

Ligand-Free Palladium-Mediated Site-Specific Protein Labeling Inside Gram-Negative Bacterial Pathogens

Li, J., Lin, S., Wang, J., Jia, S., Yang, M., Hao, Z., Zhang, X., & Chen, P. R. (2013) · Journal of the American Chemical Society · doi:10.1021/ja402424j · Cited by 172

Dimerization in GPCR mobility and signaling

Lohse, M. J. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.10.007 · Cited by 172

Conformational dynamics of a class C G-protein-coupled receptor

Vafabakhsh, R., Levitz, J., & Isacoff, E. Y. (2015) · Nature · doi:10.1038/nature14679 · Cited by 171

Conformational Changes in Rhodopsin

Dunham, T. D., & Farrens, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1683 · Cited by 170

Many-membered Carbon Rings. VII. Cycloöctyne

Blomquist, A. T., & Liu, L. H. (1953) · Journal of the American Chemical Society · doi:10.1021/ja01105a039 · Cited by 169

Amino and Carboxyl Terminal Modifications to Facilitate the Production and Purification of a G Protein-Coupled Receptor

Kobilka, B. K. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1533 · Cited by 166

Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis

Loening, A. M., Fenn, T. D., & Gambhir, S. S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.078 · Cited by 164

A Genetically Encoded Norbornene Amino Acid for the Mild and Selective Modification of Proteins in a Copper‐Free Click Reaction

Kaya, E., Vrábel, M., Deiml, C. A., Prill, S., Fluxà, V. S., & Carell, T. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201109252 · Cited by 164

Genetic code expansion in stable cell lines enables encoded chromatin modification

Elsässer, S. J., Ernst, R. J., Walker, O. S., & Chin, J. W. (2016) · Nature Methods · doi:10.1038/nmeth.3701 · Cited by 164

Site-specific Incorporation of Keto Amino Acids into Functional G Protein-coupled Receptors Using Unnatural Amino Acid Mutagenesis

Ye, S., Köhrer, C., Huber, T., Kazmi, M. A., Sachdev, P., Yan, E. C. Y., Bhagat, A., RajBhandary, U. L., & Sakmar, T. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707355200 · Cited by 163

High Constitutive Activity Is an Intrinsic Feature of Ghrelin Receptor Protein

Damian, M., Marie, J., Leyris, J.-P., Fehrentz, J., Verdié, P., Martínez, J., Banères, J., & Mary, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288324 · Cited by 159

G Protein-coupled Receptor (GPCR) Signaling via Heterotrimeric G Proteins from Endosomes

Tsvetanova, N. G., Irannejad, R., & von Zastrow, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.617951 · Cited by 159

The Power of Fluorogenic Probes

Nadler, A., & Schultz, C. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201209733 · Cited by 159

Mapping Light-Dependent Structural Changes in the Cytoplasmic Loop Connecting Helixes C and D in Rhodopsin: A Site-Directed Spin Labeling Study

Farahbakhsh, Z. T., Ridge, K. D., Khorana, H. G., & Hubbell, W. L. (1995) · Biochemistry · doi:10.1021/bi00027a033 · Cited by 159

Preparation of site-specifically labeled fluorinated proteins for 19F-NMR structural characterization

Hammill, J. T., Miyake-Stoner, S. J., Hazen, J. L., Jackson, J. C., & Mehl, R. A. (2007) · Nature Protocols · doi:10.1038/nprot.2007.379 · Cited by 158

Stability of Bacteriorhodopsin α-Helices and Loops Analyzed by Single-Molecule Force Spectroscopy

Müller, D. J., Kessler, M., Oesterhelt, F., Möller, C., Oesterhelt, D., & Gaub, H. E. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75358-7 · Cited by 158

One, two or three? Probing the stoichiometry of membrane proteins by single-molecule localization microscopy

Fricke, F., Beaudouin, J., Eils, R., & Heilemann, M. (2015) · Scientific Reports · doi:10.1038/srep14072 · Cited by 158

Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity

Xiang, Z., Ren, H., Hu, Y., Coin, I., Wei, J., Cang, H., & Wang, L. (2013) · Nature Methods · doi:10.1038/nmeth.2595 · Cited by 157

Fluorogenic Azidofluoresceins for Biological Imaging

Shieh, P., Hangauer, M. J., & Bertozzi, C. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja308203h · Cited by 157

Cell Surface Expression of α1D-Adrenergic Receptors Is Controlled by Heterodimerization with α1B-Adrenergic Receptors

Hague, C., Uberti, M. A., Chen, Z., Hall, R. A., & Minneman, K. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314014200 · Cited by 157

Cholesterol increases kinetic, energetic, and mechanical stability of the human β 2 -adrenergic receptor

Zocher, M., Zhang, C., Rasmussen, S. G. F., Kobilka, B. K., & Müller, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210373109 · Cited by 156

Single-molecule imaging revealed dynamic GPCR dimerization

Kasai, R. S., & Kusumi, A. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.11.008 · Cited by 154

Fungal recognition is mediated by the association of dectin-1 and galectin-3 in macrophages

Esteban, A., Popp, M. W., Vyas, V. K., Strijbis, K., Ploegh, H. L., & Fink, G. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111415108 · Cited by 154

Real-time trafficking and signaling of the glucagon-like peptide-1 receptor

Roed, S. N., Wismann, P., Underwood, C. R., Kulahin, N., Iversen, H., Cappelen, K. A., Schäffer, L., Lehtonen, J., Hecksher-Soerensen, J., Secher, A., et al. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.11.010 · Cited by 153

Site-directed Mutagenesis of β-Adrenergic Receptors

Fraser, C. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60524-1 · Cited by 152

An improved surface passivation method for single-molecule studies

Hua, B., Han, K. Y., Zhou, R., Kim, H., Shi, X., Abeysirigunawardena, S. C., Jain, A., Singh, D., Aggarwal, V., Woodson, S. A., et al. (2014) · Nature Methods · doi:10.1038/nmeth.3143 · Cited by 151

A Fluorescent Ligand-Binding Alternative Using Tag-lite® Technology

Zwier, J. M., Roux, T., Cottet, M., Durroux, T., Douzon, S., Bdioui, S., Gregor, N., Bourrier, E., Oueslati, N., Nicolas, L., et al. (2010) · SLAS DISCOVERY · doi:10.1177/1087057110384611 · Cited by 150

Single-Molecule Spectroscopy and Imaging of Biomolecules in Living Cells

Lord, S. J., Lee, H. D., & Moerner, W. E. (2010) · Analytical Chemistry · doi:10.1021/ac9024889 · Cited by 148

Eight years of single-molecule localization microscopy

Klein, T., Proppert, S., & Sauer, M. (2014) · Histochemistry and Cell Biology · doi:10.1007/s00418-014-1184-3 · Cited by 146

G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats

Chini, B., & Parenti, M. D. (2009) · Journal of Molecular Endocrinology · doi:10.1677/jme-08-0114 · Cited by 146

A Genetically Encoded Spin Label for Electron Paramagnetic Resonance Distance Measurements

Schmidt, M. J., Borbas, J., Drescher, M., & Summerer, D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411535q · Cited by 145

Watching conformational- and photodynamics of single fluorescent proteins in solution

Goldsmith, R. H., & Moerner, W. E. (2010) · Nature Chemistry · doi:10.1038/nchem.545 · Cited by 142

Agonist-induced Conformational Changes at the Cytoplasmic Side of Transmembrane Segment 6 in the β2 Adrenergic Receptor Mapped by Site-selective Fluorescent Labeling

Jensen, A. D., Guarnieri, F., Rasmussen, S. G. F., Asmar, F., Ballesteros, J. A., & Gether, U. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004871200 · Cited by 141

Single molecule imaging reveals a major role for diffusion in the exploration of ciliary space by signaling receptors

Ye, F., Breslow, D. K., Koslover, E. F., Spakowitz, A. J., Nelson, W. J., & Nachury, M. V. (2013) · eLife · doi:10.7554/elife.00654 · Cited by 141

Selective chemical labeling of proteins in living cells

Miller, L. W., & Cornish, V. W. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.12.007 · Cited by 140

A New Functional Suppressor tRNA/Aminoacyl−tRNA Synthetase Pair for the in Vivo Incorporation of Unnatural Amino Acids into Proteins

Wang, L., Magliery, T. J., Liu, D. R., & Schultz, P. G. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000595y · Cited by 138

The direct genetic encoding of pyrrolysine

Krzycki, J. A. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.10.009 · Cited by 137

Controlling Brownian motion of single protein molecules and single fluorophores in aqueous buffer

Cohen, A. E., & Moerner, W. E. (2008) · Optics Express · doi:10.1364/oe.16.006941 · Cited by 137

Electrokinetic trapping at the one nanometer limit

Fields, A. P., & Cohen, A. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103554108 · Cited by 136

The Chemistry of Small-Molecule Fluorogenic Probes

Grimm, J. B., Heckman, L. M., & Lavis, L. D. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-386932-6.00001-6 · Cited by 136

Multiple Active States and Oligomerization of CCR5 Revealed by Functional Properties of Monoclonal Antibodies

Blanpain, C., Vanderwinden, J., Cihak, J., Wittamer, V., Poul, E. L., Issafras, H., Stangassinger, M., Vassart, G., Marullo, S., Schlöndorff, D., et al. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-03-0129 · Cited by 135

Probing the Structure and Function of the Tachykinin Neurokinin-2 Receptor through Biosynthetic Incorporation of Fluorescent Amino Acids at Specific Sites

Turcatti, G., Nemeth, K., Edgerton, M. D., Meseth, U., Talabot, F., Peitsch, M. C., Knowles, J., Vogel, H., & Chollet, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19991 · Cited by 134

Fluorescent approaches for understanding interactions of ligands with G protein coupled receptors

Sridharan, R., Zuber, J., Connelly, S. M., Mathew, E., & Dumont, M. E. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.09.005 · Cited by 133

THE THERMAL STABILITY OF RHODOPSIN AND OPSIN

Hubbard, R. (1958) · The Journal of General Physiology · doi:10.1085/jgp.42.2.259 · Cited by 133

The bright future of single-molecule fluorescence imaging

Juette, M. F., Terry, D. S., Wasserman, M. R., Zhou, Z., Altman, R. B., Zheng, Q., & Blanchard, S. C. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2014.05.010 · Cited by 132

Protein−Protein Interaction Detection in Vitro and in Cells by Proximity Biotinylation

Fernández-Suárez, M., Chen, T. S., & Ting, A. Y. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801445p · Cited by 131

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Lameh, J., Philip, M., Sharma, Y. K., Moro, O., Ramachandran, J., & Sadée, W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42225-9 · Cited by 129

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Bertrand, L., Parent, S., Caron, M., Legault, M., Joly, E. C., Angers, S., Bouvier, M., Brown, M., Houle, B., & Ménard, L. (2002) · Journal of Receptors and Signal Transduction · doi:10.1081/rrs-120014619 · Cited by 129

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Zhang, Y. (2008) · Shengming kexue

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