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
Potent Inhibition of HIV-1 Infectivity in Macrophages and Lymphocytes by a Novel CCR5 Antagonist
Simmons, G., Clapham, P. R., Picard, L., Offord, R. E., ROSENKILDE, M. M., Schwartz, T. W., Buser, R., Wells, T. N. C., & Proudfoot, A. E. I. (1997) · Science · doi:10.1126/science.276.5310.276 · Cited by 608
Association of β-Arrestin with G Protein-coupled Receptors during Clathrin-mediated Endocytosis Dictates the Profile of Receptor Resensitization
Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., & Caron, M. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32248 · Cited by 567
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
Self-citation
Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-β-arrestin complexes after receptor endocytosis
Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., & Caron, M. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101450200 · Cited by 455
Molecular Cloning and Functional Characterization of a Novel Human CC Chemokine Receptor (CCR5) for RANTES, MIP-1β, and MIP-1α
Raport, C. J., Gosling, J., Schweickart, V. L., Gray, P. W., & Charo, I. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17161 · Cited by 448
Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling
Shenoy, S. K., & Lefkowitz, R. J. (2003) · Biochemical Journal · doi:10.1042/bj20031076 · Cited by 402
Target validation of G-protein coupled receptors
Wise, A., Gearing, K. L., & Rees, S. (2002) · Drug Discovery Today · doi:10.1016/s1359-6446(01)02131-6 · Cited by 367
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
The molecular acrobatics of arrestin activation
Gurevich, V. V., & Gurevich, E. V. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2003.12.008 · Cited by 354
Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
Angers, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.060590697 · Cited by 341
Oxytocin and Vasopressin V1a and V2 Receptors Form Constitutive Homo- and Heterodimers during Biosynthesis
Terrillon, S., Durroux, T., Mouillac, B., Breit, A., Ayoub, M. A., Taulan‐Cadars, M., Jockers, R., Barberis, C., & Bouvier, M. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0222 · Cited by 323
Self-citation
Clathrin-mediated endocytosis: membrane factors pull the trigger
Takei, K., & Haucke, V. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02082-7 · Cited by 311
SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo
Strizki, J., Xu, S., Wagner, N., Wojcik, L., Liu, J., Hou, Y., Endres, M. J., Palani, A., Shapiro, S., Clader, J. W., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221375398 · Cited by 299
Trafficking of the HIV Coreceptor CXCR4
Orsini, M. J., Parent, J., Mundell, S. J., & Benovic, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.31076 · Cited by 264
GPCR interacting proteins (GIP)
Bockaert, J., Fagni, L., Dumuis, A., & Marin, P. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.06.004 · Cited by 262
Characterization of SR 121463A, a highly potent and selective, orally active vasopressin V2 receptor antagonist.
Gal, C. S., Lacour, C., Valette, G., Garcia, G., Foulon, L., Galindo, G., Bankir, L., Pouzet, B., Guillon, G., Barberis, C., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119098 · Cited by 249
β-Arrestin Differentially Regulates the Chemokine Receptor CXCR4-mediated Signaling and Receptor Internalization, and This Implicates Multiple Interaction Sites between β-Arrestin and CXCR4
Cheng, Z.-J. J., Zhao, J., Sun, Y., Hu, W., Wu, Y., Cen, B., Wu, G., & Pei, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2479 · Cited by 236
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
Self-citation
Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
Ramsay, D., Kellett, E., McVey, M., Stephen, R. E. E. S., & Milligan, G. (2002) · Biochemical Journal · doi:10.1042/bj20020251 · Cited by 203
Defects in G Protein-Coupled Signal Transduction in Human Disease
Spiegel, A. M. (1996) · Annual Review of Physiology · doi:10.1146/annurev.ph.58.030196.001043 · Cited by 195
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
Spontaneous and Ligand-induced Trafficking of CXC-Chemokine Receptor 4
Tarasova, N. I., Stauber, R. H., & Michejda, C. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.15883 · Cited by 164
Monitoring the formation of dynamic G-protein-coupled receptor–protein complexes in living cells
Pfleger, K. D. G., & Eidne, K. A. (2005) · Biochemical Journal · doi:10.1042/bj20041361 · Cited by 160
Characterization of Sequence Determinants within the Carboxyl-terminal Domain of Chemokine Receptor CCR5 That Regulate Signaling and Receptor Internalization
Kraft, K., Olbrich, H., Majoul, I. V., Mack, M., Proudfoot, A. E. I., & Oppermann, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102782200 · Cited by 159
Pathways for internalization and recycling of the chemokine receptor CCR5
Müeller, A., Kelly, E., & Strange, P. G. (2002) · Blood · doi:10.1182/blood.v99.3.785 · Cited by 159
Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with β-arrestin and their trafficking patterns
Terrillon, S., Barberis, C., & Bouvier, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305322101 · Cited by 158
Self-citation
Hetero-oligomerization between β2- and β3-Adrenergic Receptors Generates a β-Adrenergic Signaling Unit with Distinct Functional Properties
Breit, A., Lagacé, M., & Bouvier, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313310200 · Cited by 153
Self-citation
Palmitoylation-dependent Control of Degradation, Life Span, and Membrane Expression of the CCR5 Receptor
Percherancier, Y., Planchenault, T., Valenzuela-Fernández, A., Virelizier, J., Arenzana‐Seisdedos, F., & Bachelerie, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104013200 · Cited by 151
Palmitoylation of CCR5 Is Critical for Receptor Trafficking and Efficient Activation of Intracellular Signaling Pathways
Blanpain, C., Wittamer, V., Vanderwinden, J., Boom, A., Renneboog, B., Lee, B., Poul, E. L., Asmar, L. E., Govaerts, C., Vassart, G., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100583200 · Cited by 141
Regulation of stably transfected platelet activating factor receptor in RBL-2H3 cells. Role of multiple G proteins and receptor phosphorylation.
Ali, H., Richardson, R. M., Tomhave, E. D., DuBose, R. A., Haribabu, B., & D, R. S. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31428-x · Cited by 139
THE BRET2/ARRESTIN ASSAY IN STABLE RECOMBINANT CELLS: A PLATFORM TO SCREEN FOR COMPOUNDS THAT INTERACT WITH G PROTEIN-COUPLED RECEPTORS (GPCRS)*
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
Self-citation
Phosphorylation‐independent desensitization of GABAB receptor by GRK4
Perroy, J., Adam, L., Qanbar, R., Chénier, S., & Bouvier, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg383 · Cited by 126
Self-citation
Distinct Mechanisms of Agonist-induced Endocytosis for Human Chemokine Receptors CCR5 and CXCR4
Venkatesan, S., Rose, J. J., Lodge, R., Murphy, P. M., & Foley, J. F. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0714 · Cited by 119
Applications of bioluminescence- and fluorescence resonance energy transfer to drug discovery at G protein-coupled receptors
Milligan, G. (2004) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2003.11.010 · Cited by 119
Recruitment of Activated G Protein-coupled Receptors to Pre-existing Clathrin-coated Pits in Living Cells
Scott, M. G. H., Benmerah, A., Muntaner, O., & Marullo, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106586200 · Cited by 105
β-Arrestin Binding to CC Chemokine Receptor 5 Requires Multiple C-terminal Receptor Phosphorylation Sites and Involves a Conserved Asp-Arg-Tyr Sequence Motif
Hüttenrauch, F., Nitzki, A., Lin, F., Höning, S., & Oppermann, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204033200 · Cited by 100
The Third Intracellular Loop of α2-Adrenergic Receptors Determines Subtype Specificity of Arrestin Interaction
DeGraff, J. L., Gurevich, V. V., & Benovic, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207495200 · Cited by 96
Palmitoylation of the V2 Vasopressin Receptor Carboxyl Tail Enhances β-Arrestin Recruitment Leading to Efficient Receptor Endocytosis and ERK1/2 Activation
Charest, P. G., & Bouvier, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306589200 · Cited by 92
Self-citation
Development of a BRET2 Screening Assay Using β-Arrestin 2 Mutants
Vrecl, M., Jørgensen, R., Pogačnik, A., & Heding, A. (2004) · SLAS DISCOVERY · doi:10.1177/1087057104263212 · Cited by 85
The Use of Bioluminescence Resonance Energy Transfer 2 to Study Neuropeptide Y Receptor Agonist-Induced β-Arrestin 2 Interaction
Berglund, M. M., Schober, D. A., Statnick, M. A., McDonald, P. H., & Gehlert, D. R. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.051227 · Cited by 80
Oligomerization of Wild Type and Nonfunctional Mutant Angiotensin II Type I Receptors Inhibits Gαq Protein Signaling but Not ERK Activation
Hansen, J. L., Theilade, J., Haunsø, S., & Sheikh, S. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400092200 · Cited by 79
Homo- and Hetero-oligomerization of Thyrotropin-releasing Hormone (TRH) Receptor Subtypes
Hanyaloglu, A. C., Seeber, R. M., Kohout, T. A., Lefkowitz, R. J., & Eidne, K. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209340200 · Cited by 78
Real-Time Detection of Interactions between the Human Oxytocin Receptor and G Protein-Coupled Receptor Kinase-2
Hasbi, A., Devost, D., Laporte, S. A., & Zingg, H. H. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0440 · Cited by 78
Five-transmembrane domains appear sufficient for a G protein-coupled receptor: Functional five-transmembrane domain chemokine receptors
Ling, K., Wang, P., Zhao, J., Wu, Y., Cheng, Z.-J. J., Wu, G., Hu, W., Ma, L., & Pei, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.7922 · Cited by 76
A Membrane-proximal Basic Domain and Cysteine Cluster in the C-terminal Tail of CCR5 Constitute a Bipartite Motif Critical for Cell Surface Expression
Venkatesan, S., Petrovic, A., Locati, M., Kim, Y., Weissman, D., & Murphy, P. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105722200 · Cited by 63
Arrestin-Independent Internalization of G Protein-Coupled Receptors
van Koppen, C. J., & Jakobs, K. H. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.003822 · Cited by 63
Agonist-induced Internalization of the Platelet-activating Factor Receptor Is Dependent on Arrestins but Independent of G-protein Activation
Chen, Z., Dupré, D. J., Gouill, C. L., Rola‐Pleszczynski, M., & Staňková, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110058200 · Cited by 54
Use of the BRET 7TM receptor/β-arrestin assay in drug discovery and screening
Heding, A. (2004) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.4.3.403 · Cited by 37
Fluorescent and biotinylated linear peptides as selective bifunctional ligands for the V1a vasopressin receptor
Howl, J., Wang, X. F., Kirk, C. J., & Wheatley, M. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17811.x · Cited by 30

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

See all 184

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