Cited by 184Receptor Mechanisms and Signalingbioluminescence and chemiluminescence researchChemokine receptors and signaling

The DOI matches its Crossref record; 59 of the 60 references it cites were found in a registry or an index.

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

Open access

Hamdan, Fadi F., Audet, Martin, Garneau, Philippe, Pelletier, Jerry, Bouvier, Michel·2005·SLAS Discovery

DOI 10.1177/1087057105275344

Open this paper in CoChat — free account

Abstract

In this study, the authors developed HEK293 cell lines that stably coexpressed optimal amounts of beta-arrestin2-Rluc and VENUS fusions of G protein-coupled receptors (GPCRs) belonging to both class A and class B receptors, which include receptors that interact transiently or stably with beta-arrestins. This allowed the use of a bioluminescence resonance energy transfer (BRET) 1- beta-arrestin2 translocation assay to quantify receptor activation or inhibition. One of the developed cell lines coexpressing CCR5-VENUS and beta-arrestin2- Renilla luciferase was then used for high-throughput screening (HTS) for antagonists of the chemokine receptor CCR5, the primary co-receptor for HIV. A total of 26,000 compounds were screened for inhibition of the agonist-promoted beta-arrestin2 recruitment to CCR5, and 12 compounds were found to specifically inhibit the agonist-induced beta-arrestin2 recruitment to CCR5. Three of the potential hits were further tested using other functional assays, and their abilities to inhibit CCR5 agonist-promoted signaling were confirmed. This is the 1st study describing a BRET1-beta-arrestin recruitment assay in stable mammalian cells and its successful application in HTS for GPCRs antagonists.

Integrity signals

Registry

Crossref · 10.1177/1087057105275344

Cites

59 of 59 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays.
Zhang, J.-H., Chung, T. D. Y., & Oldenburg, K. R. (1999) · SLAS Discovery · doi:10.1177/108705719900400206 · Cited by 6,847
Homozygous Defect in HIV-1 Coreceptor Accounts for Resistance of Some Multiply-Exposed Individuals to HIV-1 Infection
Liu, R., Paxton, W. A., Choe, S., Ceradini, D., Martin, S. R., Horuk, R., MacDonald, M. E., Stuhlmann, H., Koup, R. A., & Landau, N. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80110-5 · Cited by 3,074
A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K., & Miyawaki, A. (2002) · Nature Biotechnology · doi:10.1038/nbt0102-87 · Cited by 2,769
Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
Berger, E. A., Murphy, P. M., & Farber, J. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.657 · Cited by 2,180
Differential Affinities of Visual Arrestin, βArrestin1, and βArrestin2 for G Protein-coupled Receptors Delineate Two Major Classes of Receptors
Oakley, R. H., Laporte, S. A., Holt, J. A., Caron, M. G., & Barak, L. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910348199 · Cited by 882
The G protein-coupled receptor repertoires of human and mouse
Vassilatis, D. K., Hohmann, J. G., Zeng, H., Li, F., Ranchalis, J., Mortrud, M. T., Brown, A., Rodriguez, S. S., Weller, J. R., Wright, A. C., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0230374100 · Cited by 801
AMD3100, a small molecule inhibitor of HIV-1 entry via the CXCR4 co-receptor
Donzella, G. A., Schols, D., Lin, S. W., Esté, J. A., Nagashima, K. A., Maddon, P. J., Allaway, G. P., Sakmar, T. P., Henson, G. W., Clercq, E. D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-072 · Cited by 761
A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity
Baba, M., Nishimura, O., Kanzaki, N., Okamoto, M., Sawada, H., Iizawa, Y., Shiraishi, M., Aramaki, Y., Okonogi, K., Ogawa, Y., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5698 · Cited by 752
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
Self-citation
A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
Xu, Y. Q., Piston, D. W., & Johnson, C. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.151 · Cited by 613

Show all 60 references

Sorted by citations

High-throughput screening assays for the identification of chemical probes
Inglese, J., Johnson, R. L., Simeonov, A. M., Xia, M., Zheng, W., Austin, C. P., & Auld, D. S. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.17 · Cited by 632
Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery
Kenakin, T., & Miller, L. J. (2010) · Pharmacological Reviews · doi:10.1124/pr.108.000992 · Cited by 584
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
NanoBRET─A Novel BRET Platform for the Analysis of Protein–Protein Interactions
Machleidt, T., Woodroofe, C. C., Schwinn, M. K., Méndez, J., Robers, M. B., Zimmerman, K., Otto, P., Daniels, D. L., Kirkland, T. A., & Wood, K. V. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00143 · Cited by 504
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497
Crystal Structure of an LSD-Bound Human Serotonin Receptor
Wacker, D., Wang, S., McCorvy, J. D., Betz, R. M., Venkatakrishnan, A., Levit, A., Lansu, K., Schools, Z. L., Che, T., Nichols, D. E., et al. (2017) · Cell · doi:10.1016/j.cell.2016.12.033 · Cited by 474
Genetically Encodable Fluorescent Biosensors for Tracking Signaling Dynamics in Living Cells
Newman, R. H., Fosbrink, M. D., & Zhang, J. (2011) · Chemical Reviews · doi:10.1021/cr100002u · Cited by 354
Tools for GPCR drug discovery
Zhang, R., & Xie, X. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.173 · Cited by 337
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
AMD3100 Is a CXCR7 Ligand with Allosteric Agonist Properties
Kalatskaya, I., Berchiche, Y. A., Gravel, S., Limberg, B. J., Rosenbaum, J. S., & Heveker, N. (2009) · Molecular Pharmacology · doi:10.1124/mol.108.053389 · Cited by 309
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
Deconvolution of complex G protein–coupled receptor signaling in live cells using dynamic mass redistribution measurements
Schröder, R. J., Janssen, N., Schmidt, J., Kebig, A., Merten, N., Hennen, S., Müller, A., Blättermann, S., Mohr‐Andrä, M., Zahn, S., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1671 · Cited by 260
Functional assays for screening GPCR targets
Thomsen, W. J., Frazer, J. M., & Unett, D. J. (2005) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2005.10.008 · Cited by 226
Strategies to Discover Unexpected Targets for Drugs Active at G Protein–Coupled Receptors
Allen, J. A., & Roth, B. L. (2011) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100553 · Cited by 216
Bioluminescence resonance energy transfer (BRET) for the real-time detection of protein-protein interactions
Pfleger, K. D. G., Seeber, R. M., & Eidne, K. A. (2006) · Nature Protocols · doi:10.1038/nprot.2006.52 · Cited by 215
Biased Allosteric Modulators: New Frontiers in GPCR Drug Discovery
Slosky, L. M., Caron, M. G., & Barak, L. S. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.12.005 · Cited by 214
Cell-based assays: fuelling drug discovery
Michelini, E., Cevenini, L., Mezzanotte, L., Coppa, A., & Roda, A. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3933-z · Cited by 202
NanoBRET: The Bright Future of Proximity-Based Assays
Dale, N. C., Johnstone, E. K. M., White, C. W., & Pfleger, K. D. G. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00056 · Cited by 207
The BRET technology and its application to screening assays
Bacart, J., Corbel, C., Jockers, R., Bach, S., & Couturier, C. (2008) · Biotechnology Journal · doi:10.1002/biot.200700222 · Cited by 178
Cellular assays as portals to seven-transmembrane receptor-based drug discovery
Kenakin, T. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2838 · Cited by 158
Pharmacological Characterization of Membrane-Expressed Human Trace Amine-Associated Receptor 1 (TAAR1) by a Bioluminescence Resonance Energy Transfer cAMP Biosensor
Barak, L. S., Salahpour, A., Zhang, X.-D., Masri, B., Sotnikova, T. D., Ramsey, A. J., Violin, J. D., Lefkowitz, R. J., Caron, M. G., & Gainetdinov, R. R. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.048884 · Cited by 155
G-protein-coupled receptor heterodimers: pharmacology, function and relevance to drug discovery
Milligan, G. (2006) · Drug Discovery Today · doi:10.1016/j.drudis.2006.04.007 · Cited by 139
Minireview: More Than Just a Hammer: Ligand “Bias” and Pharmaceutical Discovery
Luttrell, L. M. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1314 · Cited by 136
Design and Functional Characterization of a Novel, Arrestin-Biased Designer G Protein-Coupled Receptor
Nakajima, K., & Wess, J. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.080358 · Cited by 129
BRET analysis of GPCR oligomerization: newer does not mean better
Bouvier, M., Heveker, N., Jockers, R., Marullo, S., & Milligan, G. (2006) · Nature Methods · doi:10.1038/nmeth0107-3 · Cited by 128
Self-citation
A brief review of bioluminescent systems (2019)
Fleiss, A., & Sarkisyan, K. S. (2019) · Current Genetics · doi:10.1007/s00294-019-00951-5 · Cited by 124
Quantitative assessment of constitutive G protein–coupled receptor activity with BRET-based G protein biosensors
Schihada, H., Shekhani, R., & Schulte, G. (2021) · Science Signaling · doi:10.1126/scisignal.abf1653 · Cited by 127
BRET biosensors to study GPCR biology, pharmacology, and signal transduction
Salahpour, A. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00105 · Cited by 123
Bioluminescence resonance energy transfer–based imaging of protein–protein interactions in living cells
Kobayashi, H., Picard, L.-P., Schönegge, A.-M., & Bouvier, M. (2019) · Nature Protocols · doi:10.1038/s41596-019-0129-7 · Cited by 117
Self-citation
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Arrestin-Dependent and -Independent Internalization of G Protein–Coupled Receptors: Methods, Mechanisms, and Implications on Cell Signaling
Moo, E. V., van Senten, J. R., Bräuner‐Osborne, H., & Møller, T. C. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.120.000192 · Cited by 122
β-Arrestin2-Mediated Internalization of Mammalian Odorant Receptors
Mashukova, A., Spehr, M., Hatt, H. H., & Neuhaus, E. M. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2897-06.2006 · Cited by 110
Functional Selectivity of Natural and Synthetic Prostaglandin EP4 Receptor Ligands
Leduc, M., Breton, B., Galès, C., Gouill, C. L., Bouvier, M., Chemtob, S., & Heveker, N. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.156398 · Cited by 111
Self-citation
Identification of novel species-selective agonists of the G-protein-coupled receptor GPR35 that promote recruitment of β-arrestin-2 and activate Gα13
Jenkins, L., Brea, J. M., Smith, N. J., Hudson, B. D., Reilly, G., Bryant, N. J., Castro, M., Loza, M. I., & Milligan, G. (2010) · Biochemical Journal · doi:10.1042/bj20101287 · Cited by 111
CXC Chemokine Receptor 3 Alternative Splice Variants Selectively Activate Different Signaling Pathways
Berchiche, Y. A., & Sakmar, T. P. (2016) · Molecular Pharmacology · doi:10.1124/mol.116.105502 · Cited by 110
BRET3: a red‐shifted bioluminescence resonance energy transfer (BRET)‐based integrated platform for imaging protein‐protein interactions from single live cells and living animals
De, A., Ray, P., Loening, A. M., & Gambhir, S. S. (2009) · The FASEB Journal · doi:10.1096/fj.08-118919 · Cited by 106
Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein–protein interactions in live cells
Pfleger, K. D. G., Dromey, J. R., Dalrymple, M. B., Lim, E. M. L., Thomas, W. G., & Eidne, K. A. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.01.004 · Cited by 102
Monitoring Protein‐Protein Interactions in Living Cells by Bioluminescence Resonance Energy Transfer ( BRET )
Hamdan, F. F., Percherancier, Y., Breton, B., & Bouvier, M. (2006) · Current Protocols in Neuroscience · doi:10.1002/0471142301.ns0523s34 · Cited by 102
Self-citation
Agonist-Biased Signaling via Proteinase Activated Receptor-2: Differential Activation of Calcium and Mitogen-Activated Protein Kinase Pathways
Ramachandran, R., Mihara, K., Mathur, M., Rochdi, M. D., Bouvier, M., DeFea, K., & Hollenberg, M. D. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.055509 · Cited by 100
Self-citation
Physiological and pharmacological implications of beta-arrestin regulation
Schmid, C. L., & Bohn, L. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.11.005 · Cited by 99
Biased Agonism at G Protein‐Coupled Receptors: The Promise and the Challenges—A Medicinal Chemistry Perspective
Shonberg, J., Lopez, L., Scammells, P. J., Christopoulos, A., Capuano, B., & Lane, J. R. (2014) · Medicinal Research Reviews · doi:10.1002/med.21318 · Cited by 101
Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization
Ayoub, M. A., & Pfleger, K. D. G. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.09.012 · Cited by 95
Demonstration of Improvements to the Bioluminescence Resonance Energy Transfer (BRET) Technology for the Monitoring of G Protein–Coupled Receptors in Live Cells
Kočan, M., See, H. B., Seeber, R. M., Eidne, K. A., & Pfleger, K. D. G. (2008) · SLAS DISCOVERY · doi:10.1177/1087057108324032 · Cited by 92
FRET and colocalization analyzer—A method to validate measurements of sensitized emission FRET acquired by confocal microscopy and available as an ImageJ Plug‐in
Hachet‐Haas, M., Converset, N., Marchal, O., Matthes, H. W. D., Gioria, S., Galzi, J., & Lecat, S. (2006) · Microscopy Research and Technique · doi:10.1002/jemt.20376 · Cited by 91
Thrombin-Mediated Direct Activation of Proteinase-Activated Receptor-2: Another Target for Thrombin Signaling
Mihara, K., Ramachandran, R., Saifeddine, M., Hansen, K. K., RENAUX, B. S., Polley, D., Gibson, S., Vanderboor, C., & Hollenberg, M. D. (2016) · Molecular Pharmacology · doi:10.1124/mol.115.102723 · Cited by 88
Development and Characterization of Pepducins as Gs-biased Allosteric Agonists*
Carr, R., Du, Y., Quoyer, J., Panettieri, R. A., Janz, J. M., Bouvier, M., Kobilka, B. K., & Benovic, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.618819 · Cited by 87
Self-citation
The Peptidomimetic CXCR4 Antagonist TC14012 Recruits β-Arrestin to CXCR7
Gravel, S., Malouf, C., Boulais, P. E., Berchiche, Y. A., Oishi, S., Fujii, N., Leduc, R., Sinnett, D., & Heveker, N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.147470 · Cited by 85
Discovery and Characterization of a G Protein–Biased Agonist That Inhibits β-Arrestin Recruitment to the D2 Dopamine Receptor
Free, R. B., Chun, L. S., Moritz, A. E., Miller, B. N., Doyle, T. B., Conroy, J., Padron, A., Meade, J. A., Xiao, J., Hu, X., et al. (2014) · Molecular Pharmacology · doi:10.1124/mol.113.090563 · Cited by 86
Agonist activation of the G protein‐coupled receptor GPR35 involves transmembrane domain III and is transduced via Gα13 and β‐arrestin‐2
Jenkins, L., Alvarez‐Curto, E., Campbell, K., de Munnik, S., Canals, M., Schlyer, S., & Milligan, G. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.01082.x · Cited by 88
GPR35 as a Novel Therapeutic Target
MacKenzie, A., Lappin, J. E., Taylor, D. L., Nicklin, S. A., & Milligan, G. (2011) · Frontiers in Endocrinology · doi:10.3389/fendo.2011.00068 · Cited by 82
BRET and Time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues
Cottet, M., Faklaris, O., Maurel, D., Scholler, P., Doumazane, E., Trinquet, E., Pin, J., & Durroux, T. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00092 · Cited by 81
Refining Efficacy: Allosterism and Bias in G Protein-Coupled Receptor Signaling
Luttrell, L. M., & Kenakin, T. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-160-4_1 · Cited by 81
Minireview: Targeting GPCR Activated ERK Pathways for Drug Discovery
Eishingdrelo, H. (2013) · Current Chemical Genomics · doi:10.2174/2213988501307010009 · Cited by 80
Recruitment of β-arrestin2 to the dopamine D2 receptor: Insights into anti-psychotic and anti-parkinsonian drug receptor signaling
Klewe, I. V., Nielsen, S. M., TARPO, L., Urizar, E. T., Dipace, C., Javitch, J. A., Gether, U., Egebjerg, J., & Christensen, K. V. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.03.015 · Cited by 77
Unraveling G Protein-coupled Receptor Endocytosis Pathways Using Real-time Monitoring of Agonist-promoted Interaction between β-Arrestins and AP-2
Hamdan, F. F., Rochdi, M. D., Breton, B., Fessart, D., Michaud, D. E., Charest, P. G., Laporte, S. A., & Bouvier, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700577200 · Cited by 76
Self-citation
Application of Bioluminescence Resonance Energy Transfer (BRET) for Biomolecular Interaction Studies
Prinz, A., Diskar, M., & Herberg, F. W. (2006) · ChemBioChem · doi:10.1002/cbic.200600048 · Cited by 75
Subcellular Imaging of Dynamic Protein Interactions by Bioluminescence Resonance Energy Transfer
Coulon, V., Audet, M., Homburger, V., Bockaert, J., Fagni, L., Bouvier, M., & Perroy, J. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117275 · Cited by 73
Self-citation
A Broad G Protein-Coupled Receptor Internalization Assay that Combines SNAP-Tag Labeling, Diffusion-Enhanced Resonance Energy Transfer, and a Highly Emissive Terbium Cryptate
Levoye, A., Zwier, J. M., Jaracz‐Ros, A., Klipfel, L., Cottet, M., Maurel, D., Bdioui, S., Balabanian, K., Prézeau, L., Trinquet, E., et al. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00167 · Cited by 72
Experimental challenge to a 'rigorous' BRET analysis of GPCR oligomerization
Salahpour, A., & Masri, B. (2007) · Nature Methods · doi:10.1038/nmeth0807-599 · Cited by 70
Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist‐Induced Arrestin Recruitment to Modified and Unmodified G Protein‐Coupled Receptors
Donthamsetti, P., Quejada, J. R., Javitch, J. A., Gurevich, V. V., & Lambert, N. A. (2015) · Current Protocols in Pharmacology · doi:10.1002/0471141755.ph0214s70 · Cited by 64
Bioluminescence based in vivo screening technologies
Kelkar, M. G., & De, A. (2012) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2012.07.014 · Cited by 59
Role of SUMO in RNF4-mediated Promyelocytic Leukemia Protein (PML) Degradation
Percherancier, Y., Germain-Desprez, D., Galisson, F., Mascle, X. H., Dianoux, L., Estephan, P., Chelbi‐Alix, M. K., & Aubry, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.006387 · Cited by 62
Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology
Khamlichi, C. E., Reverchon, F., Hervouet, N., Blot, L., Reiter, É., & Morisset‐Lopez, S. (2019) · Molecules · doi:10.3390/molecules24030537 · Cited by 66
Serotonin receptor signaling and regulation via β-arrestins
Bohn, L., & Schmid, C. L. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.516741 · Cited by 60
Functional complementation of high-efficiency resonance energy transfer: a new tool for the study of protein binding interactions in living cells
Molinari, P., Casella, I., & Costa, T. (2007) · Biochemical Journal · doi:10.1042/bj20070803 · Cited by 60
Antagonists of GPR35 Display High Species Ortholog Selectivity and Varying Modes of Action
Jenkins, L., Harries, N., Lappin, J. E., Mackenzie, A. E., Neetoo‐Isseljee, Z., Southern, C., McIver, E. G., Nicklin, S. A., Taylor, D. L., & Milligan, G. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.198945 · Cited by 58
Recent progress in assays for GPCR drug discovery
Guo, S., Zhao, T., Yun, Y., & Xie, X. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00464.2021 · Cited by 53
Future and frontiers of automated screening in plant sciences
Kolukisaoglu, Ü., & Thurow, K. (2010) · Plant Science · doi:10.1016/j.plantsci.2010.03.006 · Cited by 55
Biased Ligand Modulation of Seven Transmembrane Receptors (7TMRs): Functional Implications for Drug Discovery
Correll, C. C., & McKittrick, B. A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401677g · Cited by 54
Direct evidence that the GPCR CysLTR2 mutant causative of uveal melanoma is constitutively active with highly biased signaling
Ceraudo, E., Horioka-Duplix, M., Mattheisen, J. M., Hitchman, T. D., Moore, A. R., Kazmi, M. A., Chi, P., Chen, Y., Sakmar, T. P., & Huber, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015352 · Cited by 55
Setting Up a Bioluminescence Resonance Energy Transfer High throughput Screening Assay to Search for Protein/Protein Interaction Inhibitors in Mammalian Cells
Couturier, C., & Deprez, B. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00100 · Cited by 52
The Arrestin-selective Angiotensin AT1 Receptor Agonist [Sar1,Ile4,Ile8]-AngII Negatively Regulates Bradykinin B2 Receptor Signaling via AT1-B2 Receptor Heterodimers
Wilson, P. C., Lee, M., Appleton, K. M., El‐Shewy, H. M., Morinelli, T. A., Peterson, Y. K., Luttrell, L. M., & Jaffa, A. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.472381 · Cited by 52
Visualization and Quantitative Analysis of G Protein-Coupled Receptor−β-Arrestin Interaction in Single Cells and Specific Organs of Living Mice Using Split Luciferase Complementation
Takakura, H., Hattori, M., Takeuchi, M., & Ozawa, T. (2012) · ACS Chemical Biology · doi:10.1021/cb200360z · Cited by 52
Application of G Protein-Coupled Receptor-Heteromer Identification Technology to Monitor β -Arrestin Recruitment to G Protein-Coupled Receptor Heteromers
See, H. B., Seeber, R. M., Kočan, M., Eidne, K. A., & Pfleger, K. D. G. (2010) · Assay and Drug Development Technologies · doi:10.1089/adt.2010.0336 · Cited by 52
Protein–Protein Interactions as Drug Targets
Skwarczynska, M., & Ottmann, C. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.138 · Cited by 52
Improved donor/acceptor BRET couples for monitoring β‐arrestin recruitment to G protein‐coupled receptors
Kamal, M. T., Marquez, M., Vauthier, V., Leloire, A., Froguel, P., Jockers, R., & Couturier, C. (2009) · Biotechnology Journal · doi:10.1002/biot.200900016 · Cited by 46
Techniques: New pharmacological perspectives for the leptin receptor
Peelman, F., Couturier, C., Dam, J., Zabeau, L., Tavernier, J. H., & Jockers, R. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.02.009 · Cited by 44
NanoBRET ligand binding at a GPCR under endogenous promotion facilitated by CRISPR/Cas9 genome editing
White, C. W., Johnstone, E. K. M., See, H. B., & Pfleger, K. D. G. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.11.018 · Cited by 43
Enabling systematic interrogation of protein–protein interactions in live cells with a versatile ultra-high-throughput biosensor platform
Mo, X., Luo, Y., Ivanov, A. A., Su, R., Havel, J. J., Li, Z., Khuri, F. R., Du, Y., & Fu, H. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv064 · Cited by 43
High-Throughput Identification and Characterization of Novel, Species-selective GPR35 Agonists
Neetoo‐Isseljee, Z., Mackenzie, A. E., Southern, C., Jerman, J. C., McIver, E. G., Harries, N., Taylor, D. L., & Milligan, G. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.201798 · Cited by 40
Src-dependent phosphorylation of β2-adaptin dissociates the β-arrestin–AP-2 complex
Fessart, D., Simaan, M., Zimmerman, B., Comeau, J., Hamdan, F. F., Wiseman, P. W., Bouvier, M., & Laporte, S. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.03444 · Cited by 39
Self-citation
Multiple GPCR Functional Assays Based on Resonance Energy Transfer Sensors
Zhou, Y., Meng, J., Xu, C., & Liu, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.611443 · Cited by 39
Study of GPCR–Protein Interactions by BRET
Kočan, M., & Pfleger, K. D. G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-126-0_20 · Cited by 38
Light resonance energy transfer‐based methods in the study of G protein‐coupled receptor oligomerization
Gandía, J., Lluı́s, C., Ferré, S., Franco, R., & Ciruela, F. (2007) · BioEssays · doi:10.1002/bies.20682 · Cited by 38
An update of novel screening methods for GPCR in drug discovery
Chen, L., Jin, L., & Zhou, N. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.699036 · Cited by 38
Bioluminescence Resonance Energy Transfer to Detect Protein-Protein Interactions in Live Cells
Brown, N. E., Blumer, J., & Hepler, J. R. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2425-7_30 · Cited by 37
Studying G protein-coupled receptor activation using split-tobacco etch virus assays
Djannatian, M., Galinski, S., Fischer, T. M., & Rossner, M. J. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.01.042 · Cited by 37
Functional Tuning of Photoactive Yellow Protein by Active Site Residue 46
Philip, A. F., Eisenman, K. T., Papadantonakis, G. A., & Hoff, W. D. (2008) · Biochemistry · doi:10.1021/bi801730y · Cited by 37
Monitoring interactions between G-protein-coupled receptors and β-arrestins
Pfleger, K. D. G., Dalrymple, M. B., Dromey, J. R., & Eidne, K. A. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350764 · Cited by 36
An Engineered GM-CSF-CCL2 Fusokine Is a Potent Inhibitor of CCR2-Driven Inflammation As Demonstrated in a Murine Model of Inflammatory Arthritis
Rafei, M., Berchiche, Y. A., Birman, E., Boivin, M., Young, Y. K., Wu, J. H., Heveker, N., & Galipeau, J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900523 · Cited by 36
G protein-independent cell-based assays for drug discovery on seven-transmembrane receptors
Verkaar, F., van Rosmalen, J. W. G., Blomenröhr, M., van Koppen, C. J., Blankesteijn, W. M., Smits, J. F. M., & Zaman, G. J. R. (2008) · Biotechnology annual review · doi:10.1016/s1387-2656(08)00010-0 · Cited by 36
Mathematical Models for Quantitative Assessment of Bioluminescence Resonance Energy Transfer: Application to Seven Transmembrane Receptors Oligomerization
Drinovec, L., Kubale, V., Larsen, J. N., & Vrecl, M. (2012) · Front. Endocrin. · doi:10.3389/fendo.2012.00104 · Cited by 34
First BRET‐based screening assay performed in budding yeast leads to the discovery of CDK5/p25 interaction inhibitors
Corbel, C., Wang, Q., Bousserouel, H., Hamdi, A., Zhang, B., Lozach, O., Ferandin, Y., Tan, V. B. C., Guéritte, F., Colas, P., et al. (2011) · Biotechnology Journal · doi:10.1002/biot.201100138 · Cited by 35
Investigating Internalization and Intracellular Trafficking of GPCRs: New Techniques and Real-Time Experimental Approaches
Foster, S. R., & Bräuner‐Osborne, H. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_57 · Cited by 37
Protein‐protein interactions monitored in cells from transgenic mice using bioluminescence resonance energy transfer
Audet, M., Lagacé, M., Silversides, D. W., & Bouvier, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-144816 · Cited by 32
Self-citation
The hypotensive effect of activated apelin receptor is correlated with β-arrestin recruitment
Besserer‐Offroy, É., Bérubé, P., Côté, J., Murza, A., Longpré, J., Dumaine, R., Lesur, O., Auger‐Messier, M., Leduc, R., Marsault, É., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.032 · Cited by 31
Biophysical Detection of Diversity and Bias in GPCR Function
Jaeger, W. C., Armstrong, S. P., Hill, S. J., & Pfleger, K. D. G. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00026 · Cited by 30
Endogenous Opioid Peptides and Alternatively Spliced Mu Opioid Receptor Seven Transmembrane Carboxyl-Terminal Variants
Abrimian, A., Kraft, T. T., & Pan, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073779 · Cited by 31
CCR5: Established paradigms and new frontiers for a ‘celebrity’ chemokine receptor
Scurci, I., Martins, E., & Hartley, O. (2018) · Cytokine · doi:10.1016/j.cyto.2018.02.018 · Cited by 28
Beyond Fluorescent Proteins: Hybrid and Bioluminescent Indicators for Imaging Neural Activities
Wang, A., Feng, J., Li, Y., & Zou, P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00455 · Cited by 28

Authors: Hamdan, F. F., Audet, M., Garneau, P., Pelletier, J., & Bouvier, M.
Affiliations: Université de Montréal (CA)
McGill University (CA)
ORCID: Hamdan, Fadi F.
Audet, Martin
Pelletier, Jerry
Bouvier, Michel
Venue: SLAS Discovery
Publisher: Elsevier BV
Published: 2005-08
Volume: 10
Issue: 5
Pages: 463-475
ISSN: 2472-5552 (ISSN-L)
DOI: 10.1177/1087057105275344
OpenAlex: W2094714066
Cited by: 183
References: 60
Citations by year: 2026: 2 · 2025: 4 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 9 · 2020: 8 · 2019: 6 · 2018: 8 · 2017: 5 · 2016: 6 · 2015: 17 · 2014: 8 · 2013: 8 · 2012: 16
FWCI: 4.64
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 6112 d)
Locations: SLAS DISCOVERY (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › bioluminescence and chemiluminescence research
Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
Keywords: G protein-coupled receptors, β-arrestin2, CCR5, chemokine receptor antagonists, high-throughput screening, HIV co-receptor, HEK293 cells, receptor antagonists
MeSH terms: beta-Arrestins, Animals, Automation, Calcium, Cell Line, Dose-Response Relationship, Drug, Drug Evaluation, Preclinical, Energy Transfer, HIV, Humans, Luminescent Measurements, Microscopy, Fluorescence, Plasmids, Time Factors, Genes, Reporter, Arrestins, Receptors, CCR5, Protein Transport, Receptors, G-Protein-Coupled, Macromolecular Substances, Renilla, Luciferases, Renilla, Green Fluorescent Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Citations

Cites

Cited by

Related

Metadata

Record

About these checks