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

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

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

Interactive Proteomics: What Lies Ahead?

Suter, B., Kittanakom, S., & Štagljar, I. (2008) · BioTechniques · doi:10.2144/000112799 · Cited by 27

Experimental determination of the bioluminescence resonance energy transfer (BRET) Förster distances of NanoBRET and red-shifted BRET pairs

Weihs, F., Wang, J., Pfleger, K. D. G., & Dacres, H. (2020) · Analytica Chimica Acta X · doi:10.1016/j.acax.2020.100059 · Cited by 26

To sense or not to sense—new insights from GPCR-based and arrestin-based biosensors

Haider, R. S., Godbole, A., & Hoffmann, C. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.10.005 · Cited by 25

Evolution of Class-Specific Peptides Targeting a Hot Spot of the Gαs Subunit

Austin, R. J., Ja, W. W., & Roberts, R. W. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.032 · Cited by 25

Spinophilin as a novel regulator of M 3 muscarinic receptor‐mediated insulin release in vitro and in vivo

de Azúa, I. R., Nakajima, K., Rossi, M., Cui, Y., Jou, W., Gavrilova, O., & Wess, J. (2012) · The FASEB Journal · doi:10.1096/fj.12-204644 · Cited by 24

Seeking ligand bias: assessing GPCR coupling to β-arrestins for drug discovery

Bohn, L., & McDonald, P. H. (2010) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2010.06.005 · Cited by 24

Application of BRET for Studying G Protein-Coupled Receptors

Kaczor, A. A., Makarska-Białokoz, M., Selent, J., Fuente, R., Martí-Solano, M., & Castro, M. (2014) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557514666140428113708 · Cited by 24

Mu Opioids Induce Biased Signaling at the Full-Length Seven Transmembrane C-Terminal Splice Variants of the mu Opioid Receptor Gene, Oprm1

Narayan, A., Hunkele, A., Xu, J., Bassoni, D. L., Pasternak, G. W., & Pan, Y. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00973-5 · Cited by 24

Detection of GPCR/β-Arrestin Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer Technology

Kočan, M., & Pfleger, K. D. G. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-317-6_22 · Cited by 21

The A, B, Cs of G-protein-coupled receptor pharmacology in assay development for HTS

McLoughlin, D. J., Bertelli, F., & Williams, C. (2007) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2.5.603 · Cited by 21

Quantification of Molecular Interactions in Living Cells in Real Time using a Membrane Protein Nanopattern

Reichmuth, A. M., Zimmermann, M., Wilhelm, F. M., Frutiger, A., Blickenstorfer, Y., Fattinger, C., Waldhoer, M., & Vörös, J. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00987 · Cited by 20

Visualization of ligand-induced dopamine D2S and D2L receptor internalization by TIRF microscopy

Tabor, A., Weikert, D., Hübner, H., Kornhuber, J., & Gmeiner, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-11436-1 · Cited by 24

Biochemical insights into structure and function of arrestins

Aydin, Y., & Coin, I. (2021) · FEBS Journal · doi:10.1111/febs.15811 · Cited by 19

Cell-penetrating pepducins targeting the neurotensin receptor type 1 relieve pain

Brouillette, R. L., Besserer‐Offroy, É., Mona, C. E., Chartier, M., Lavenus, S. B., Sousbie, M., Belleville, K., Longpré, J., Marsault, É., Grandbois, M., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104750 · Cited by 19

A High-Throughput Drug Screening Strategy for Detecting Rhodopsin P23H Mutant Rescue and Degradation

Chen, Y., Tang, H., Seibel, W. L., Papoian, R., Li, X., Lambert, N. A., & Palczewski, K. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-16298 · Cited by 18

BRET Biosensor Analysis of Receptor Tyrosine Kinase Functionality

Siddiqui, S., Cong, W., Daimon, C. M., Martin, B., & Maudsley, S. R. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00046 · Cited by 18

VRQ397 (CRAVKY): a novel noncompetitive V2 receptor antagonist

Řihakova, L., Quiniou, C., Hamdan, F. F., Kaul, R., Brault, S., Hou, X., Lahaie, I., Sapieha, P. S., Hamel, D., Shao, Z., et al. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90766.2008 · Cited by 18

Tissue-Based Biosensors

Acha, V., Andrews, T., Huang, Q., Sardar, D. K., & Hornsby, P. J. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0919-0_9 · Cited by 18

Design and construction of conformational biosensors to monitor ion channel activation: A prototype FlAsH/BRET-approach to Kir3 channels

Robertson, D. N., Sleno, R., Nagi, K., Pétrin, D., Hébert, T. E., & Piñeyro, G. (2015) · Methods · doi:10.1016/j.ymeth.2015.07.011 · Cited by 17

β-Arrestin-Based Bret2 Screening Assay for the “Non”-β-Arrestin Binding CB1 Receptor

Vrecl, M., Nørregaard, P. K., Almholt, D. L. C., Elster, L., Pogačnik, A., & Heding, A. (2009) · SLAS DISCOVERY · doi:10.1177/1087057109333101 · Cited by 17

Present and Future Approaches to Screening of G-Protein-Coupled Receptors

Lundstrom, K. H. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.9 · Cited by 16

GPCR Biosensors to Study Conformational Dynamics and Signaling in Drug Discovery

Saca, V. R., Burdette, C. S., & Sakmar, T. P. (2025) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-061724-080836 · Cited by 16

Cannabinoid receptor 1 ligands: Biased signaling mechanisms driving functionally selective drug discovery

Tian, L., Qiang, T., Liu, S., Zhang, B., Zhang, Y., Zhang, B., Hu, J., Zhang, J., Qi, L., Ke, C., et al. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108795 · Cited by 14

Delineating biased ligand efficacy at 7TM receptors from an experimental perspective

Galandrin, S., Onfroy, L., Poirot, M. C., Sénard, J., & Galès, C. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.04.009 · Cited by 16

Bioluminescence Resonance Energy Transfer: An Emerging Tool for the Detection of Protein–Protein Interaction in Living Cells

Gersting, S. W., Lotz-Havla, A. S., & Muntau, A. C. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-424-7_19 · Cited by 13

Kinetic and Thermodynamic Insights into Agonist Interactions with the Parathyroid Hormone Receptor-1 from a New NanoBRET Assay

Yu, Z., Cary, B. P., Kim, T. W., Nguyen, K. D., Gardella, T. J., & Gellman, S. H. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00595 · Cited by 12

Development of a High-Throughput Screening–Compatible Cell-Based Functional Assay to Identify Small Molecule Probes of the Galanin 3 Receptor (GalR3)

Robinson, J. D., Smith, A. M., Sturchler, E., Tabrizifard, S., Kamenecka, T. M., & McDonald, P. H. (2013) · Assay and Drug Development Technologies · doi:10.1089/adt.2013.526 · Cited by 15

A High-Content, Live-Cell, and Real-Time Approach to the Quantitation of Ligand-Induced β-Arrestin2 and Class A/Class B GPCR Mobilization

Leonard, A. P., Appleton, K. M., Luttrell, L. M., & Peterson, Y. K. (2013) · Microscopy and Microanalysis · doi:10.1017/s1431927612014067 · Cited by 13

Optical approaches for single-cell and subcellular analysis of GPCR–G protein signaling

Kankanamge, D., Ratnayake, K., Senarath, K., Tennakoon, M., Harmon, E., & Karunarathne, A. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01774-6 · Cited by 13

Analysis of Protein–Protein Interactions Using Bioluminescence Resonance Energy Transfer

Pfleger, K. D. G. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-321-3_14 · Cited by 13

Cell-Based Assays and Animal Models for GPCR Drug Screening

Takakura, H., Hattori, M., Tanaka, M., & Ozawa, T. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2336-6_18 · Cited by 11

Heterodimerisation of G protein-coupled receptors: implications for drug design and ligand screening

del Burgo, L. S., & Milligan, G. (2010) · Expert Opinion on Drug Discovery · doi:10.1517/17460441003720467 · Cited by 11

Bioluminescence measurements in mice using a skin window

Huang, Q., Acha, V., Yow, R. M., Schneider, E. C., Sardar, D. K., & Hornsby, P. J. (2007) · Journal of Biomedical Optics · doi:10.1117/1.2795567 · Cited by 11

Correction to: Mu Opioids Induce Biased Signaling at the Full-Length Seven Transmembrane C-Terminal Splice Variants of the mu Opioid Receptor Gene, Oprm1

Narayan, A., Hunkele, A., Xu, J., Bassoni, D. L., Pasternak, G. W., & Pan, Y. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00990-4 · Cited by 11

Monitoring Ligand-Activated Protein–Protein Interactions Using Bioluminescent Resonance Energy Transfer (BRET) Assay

Coriano, C. G., Powell, E., & Xu, W. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6346-1_1 · Cited by 10

Orphan Seven Transmembrane Receptor Screening

Wigglesworth, M. J., Wolfe, L. A., & Wise, A. (2007) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2006_006 · Cited by 10

A Real-Time, Plate-Based BRET Assay for Detection of cGMP in Primary Cells

Valkovic, A. L., Kočan, M., Hoare, B. L., Marshall, S. A., Scott, D. J., & Bathgate, R. A. D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031908 · Cited by 9

Analysis of Arrestin Recruitment to Chemokine Receptors by Bioluminescence Resonance Energy Transfer

Bonneterre, J., Montpas, N., Boularan, C., Galès, C., & Heveker, N. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.09.003 · Cited by 9

High-Throughput and In Silico Screening in Drug Discovery

Nandu, T. G., Venkatachalam, A. B., & Sugathan, S. (2017) · Springer eBooks · doi:10.1007/978-981-10-3573-9_11 · Cited by 9

A comparative analysis of resonance energy transfer methods for Alzheimer related protein–protein interactions in living cells

Kim, J., Lee, J., Kwon, D., Lee, H., & Grailhe, R. (2011) · Molecular BioSystems · doi:10.1039/c1mb05279a · Cited by 9

Characterizing Dynamic Protein–Protein Interactions Using the Genetically Encoded Split Biosensor Assay Technique Split TEV

Wintgens, J. P., Rossner, M. J., & Wehr, M. C. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6940-1_14 · Cited by 9

Ackr3-Venus knock-in mouse lights up brain vasculature

Ehrlich, A. T., Semache, M., Couvineau, P., Wojcik, S., Kobayashi, H., Thelen, M., Gross, F., Hogue, M., Gouill, C. L., Darcq, E., et al. (2021) · Molecular Brain · doi:10.1186/s13041-021-00862-y · Cited by 9

Drug discovery through biophysical techniques: Methods and applications

Zhou, Y., Hu, H., Huang, Q., Tang, Y., & Liu, Y. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108947 · Cited by 9

Molecular Mechanisms of Biased and Probe-Dependent Signaling at CXC-Motif Chemokine Receptor CXCR3 Induced by Negative Allosteric Modulators

Brox, R., Milanos, L., Saleh, N., Baumeister, P., Buschauer, A., Hofmann, D., Heinrich, M. R., Clark, T., & Tschammer, N. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.110296 · Cited by 8

Protein-Coupled Receptor

Nakajima, K., & Wess, J. (2012) · Cited by 8

Detecting Protein–Protein Interactions in Living Cells: Development of a Bioluminescence Resonance Energy Transfer Assay to Evaluate the PSD-95/NMDA Receptor Interaction

Gottschalk, M., Bach, A., Hansen, J. L., Krogsgaard‐Larsen, P., Kristensen, A. S., & Strømgaard, K. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9998-4 · Cited by 8

Monitoring G Protein-Coupled Receptor Activation Using the Protein Fragment Complementation Technique Split TEV

Wehr, M. C., Galinski, S., & Rossner, M. J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2336-6_8 · Cited by 8

High Throughput Screening

Janzen, W. P. (2008) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-60327-375-6_60 · Cited by 8

Bringing GPCR Structural Biology to Medical Applications: Insights from Both V2 Vasopressin and Mu-Opioid Receptors

Fouillen, A., Bous, J., Granier, S., Mouillac, B., & Sounier, R. (2023) · Membranes · doi:10.3390/membranes13060606 · Cited by 8

Receptor Determinants for β-Arrestin Functional Specificity at C-X-C Chemokine Receptor 5

Crecelius, J. M., Manz, A. R., Benzow, S., & Marchese, A. (2024) · Molecular Pharmacology · doi:10.1124/molpharm.124.000942 · Cited by 6

Visualization of real-time receptor endocytosis in dopamine neurons enabled by NTSR1-Venus knock-in mice

Ehrlich, A. T., Couvineau, P., Schamiloglu, S., Wojcik, S., Fonte, D. D., Mezni, A., von Zastrow, M., Bender, K. J., Bouvier, M., & Kieffer, B. L. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1076599 · Cited by 5

Bioluminescent tools for the analysis of G-protein-coupled receptor and arrestin interactions

Hattori, M., & Ozawa, T. (2015) · RSC Advances · doi:10.1039/c4ra14979c · Cited by 5

iBRET Screen of the ABCD1 Peroxisomal Network and Mutation-Induced Network Perturbations

Lotz-Havla, A. S., Woidy, M., Guder, P., Friedel, C. C., Klingbeil, J. M., Bulau, A., Schultze, A., Dahmen, I., Noll‐Puchta, H., Kemp, S., et al. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00330 · Cited by 5

In‐Cell Arrestin‐Receptor Interaction Assays

Zheng, C., Javitch, J. A., Lambert, N. A., Donthamsetti, P., & Gurevich, V. V. (2023) · Current Protocols · doi:10.1002/cpz1.890 · Cited by 6

Analysis of G Protein and β-Arrestin Activation in Chemokine Receptors Signaling

Vacchini, A., Busnelli, M., Chini, B., Locati, M., & Borroni, E. M. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.09.016 · Cited by 4

Bioluminescence Resonance Energy Transfer Approaches to Discover Bias in GPCR Signaling

Johnstone, E. K. M., & Pfleger, K. D. G. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2914-6_13 · Cited by 4

G Protein-Coupled Receptors

Thomsen, W. J., & Behan, D. P. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00062-6 · Cited by 4

New Winds in Gpcr-Based Drug Discovery

Lundstrom, K. H. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0008 · Cited by 4

Biochemical and Biophysical Analyses of Ras Modification by Ubiquitin

Terrillon, S., & Bar‐Sagi, D. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)38018-x · Cited by 3

Ligand-induced dimerization of syndecan-3 at the cell surface

Kulesskiy, E., Tumova, S., & Rauvala, H. (2013) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2013.46a006 · Cited by 3

Defining the Functional Equivalence of Wild-Type and Chemically Engineered G Protein-Coupled Receptors

Alvarez‐Curto, E., & Milligan, G. (2015) · Neuromethods · doi:10.1007/978-1-4939-2944-3_1 · Cited by 3

Biased Signaling and Its Role in the Genesis of Short- and Long-Acting β2-Adrenoceptor Agonists

Phan, N. T. N., Roman, L. B., Hoare, B. L., Harwood, C. R., Geary, N., Guba, W., Han, Y., Zenko, V., Koers, E. J., Rufer, A. C., et al. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00148 · Cited by 2

Molecular Sensors for Transcriptional and Post-Transcriptional Assays

Auld, D. S., & Thorne, N. (2012) · Cambridge University Press eBooks · doi:10.1017/cbo9781139021500.018 · Cited by 2

βArrestins: Ligand-Directed Regulators of 5-HT2A Receptor Trafficking and Signaling Events

Schmid, C. L., & Bohn, L. (2018) · Springer eBooks · doi:10.1007/978-3-319-70474-6_2 · Cited by 2

Adenoviral Sensors for High‐Content Cellular Analysis

Kendall, J. M., Ismail, R., & Thomas, N. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)14014-8 · Cited by 2

Assays to Characterize the Cellular Pharmacology of a Chemical Probe

Stefaniak, J., Galan, S. R. G., & Huber, K. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160745-00247 · Cited by 1

Évaluation de l'effet des antagonistes synthétiques du récepteur de chimiokine, CXCR4 sur CXCR7

Gravel, S. (2010) · doi:10.71781/31064

New Approaches Applied to Drug Screening

Brea, J. M., & Loza, M. I. (2012) · Wiley eBooks · doi:10.1002/9781118185537.ch14

HIGH THROUGHPUT SCREENING OF PRIMING CANDIDATES FOR IMPACT ON NONVIRAL GENE DELIVERY

Nguyen, A. (2015) · Lincoln (University of Nebraska)

Elucidating novel aspects of hypothalamic releasing hormone receptor regulation

Dromey, J. R. (2007) · UWA Profiles and Research Repository (UWA)

Detecting the Role of Arrestins in G Protein-Coupled Receptor Regulation

Bohn, L., & McDonald, P. H. (2011) · Neuromethods · doi:10.1007/978-1-61779-179-6_17

Readout Present and Near Future

(2010) · CRC Press eBooks · doi:10.1201/ebk1420073492-c9

D1 AND D2 DOPAMINE RECEPTOR BIASED AND HETEROMERIC SIGNALING: IMPLICATIONS FOR PROTEIN CONFORMATIONAL FLUIDITY

Chun, L. S. (2015)

Bioluminescence-based biosensors to study histamine receptor activity

Ma, X. (2023) · doi:10.5463/thesis.173

Engineering of Prevalent Luciferase–Luciferin Pairs Toward Tunable Light and Applications in the Field of Bioluminescence Imaging

Huang, Z., & Li, M. (2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837673117-00202

Additional file 1 of Ackr3-Venus knock-in mouse lights up brain vasculature

Ehrlich, A. T., Semache, M., Couvineau, P., Wojcik, S., Kobayashi, H., Thelen, M., Gross, F., Hogue, M., Gouill, C. L., Darcq, E., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16696540

Oligomérisation des récepteurs couplés au protéines G de la famille de la vasopressine et de l’ocytocine : mise en évidence dans les tissus natifs

Cottet, M. (2013) · theses.fr (ABES) · doi:10.70675/dfa759a2za648z4614zba18zf0541f9ca2eb

Structure quaternaire des récepteurs de chimiokines CXCR4 et CCR2 et interaction avec leur effecteurs.

Armando, S. (2010) · theses.fr (ABES) · doi:10.70675/d5e86fe8z4b1dz4535z8a41zee2eeb513d50

Méthodes RMN pour la découverte de nouveaux ligands ciblant les récepteurs couplés aux protéines G

Raingeval, C. (2019) · theses.fr (ABES) · doi:10.70675/8b962ab5z793az4112z84e4zbc9f4e566f31

Développement d’un système rapporteur générique sensible, au double mode de lecture BRET/HCS, pour l’étude du suivi de gènes rapporteurs, de l’activité de protéase virale et des interactions protéine-protéine

Colin, B. (2018) · doi:10.70675/76d6d043z6093z4398z9dadz7e3f9ba0d7ef

Dose et cofacteurs des protéines Hox lors du développement des organes de vol chez les insectes

Giraud, G. (2020) · theses.fr (ABES) · doi:10.70675/50757190zb2d8z4fc2zbc96zfea34ff0071c

Peroxisomal interactome mapping enables network-based modelling of function and disease

Gersting, S. W., Cramer, J. V., Guder, P., Lotz-Havla, A. S., Wolf, B., Noll‐Puchta, H., Erdmann, R., Muntau, A. C., & Woidy, M. (2026) · Life Science Alliance · doi:10.26508/lsa.202503562

BindingDB Entry 50045075: Biased ligand modulation of seven transmembrane receptors (7TMRs): functional implications for drug discovery.

BindingDB (2016) · UC San Diego · doi:10.7270/q2th8pb1

Structural and functional insights into rhodopsin‐like and secretin‐like GPCR –arrestin interactions and regulation

Gupta, V., & Beck‐Sickinger, A. G. (2026) · FEBS Journal · doi:10.1111/febs.70772

Establishment of a new cell line for high-throughput evaluation of chemokine CCR5 receptor antagonists.

Ji, L., Sheng, Y., Chen, L., & Wang, Z. (2009) · PubMed · Cited by 1

Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist‐Induced Arrestin Recruitment to Modified and Unmodified G Protein‐Coupled Receptors

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