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

The Physiology of Glucagon-like Peptide 1

Holst, J. J. (2007) · Physiological Reviews · doi:10.1152/physrev.00034.2006 · Cited by 3,371

Pathways and mechanisms of endocytic recycling

Grant, B. D., & Donaldson, J. G. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2755 · Cited by 1,424

Molecular and Cellular Endocrinology

Rainey, W. E., & Rodgers, R. J. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.10.007 · Cited by 1,340

GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus

Meier, J. J. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.140 · Cited by 1,311

Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.

Kieffer, T. J., McIntosh, C. H., & Pederson, R. A. (1995) · Endocrinology · doi:10.1210/endo.136.8.7628397 · Cited by 1,124

Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells.

Göke, R., Fehmann, H. C., Linn, T., Schmidt, H., Krause, M., Eng, J., & Göke, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36565-2 · Cited by 837

Conformational biosensors reveal GPCR signalling from endosomes

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

Regulation of GPCRs by Endocytic Membrane Trafficking and Its Potential Implications

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

International Union of Pharmacology. XXXV. The Glucagon Receptor Family

Mayo, K. E., Miller, L. J., BATAILLE, D., Dalle, S., Göke, B., Thorens, B., & Drucker, D. J. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.6 · Cited by 514

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

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

The arcuate nucleus mediates GLP-1 receptor agonist liraglutide-dependent weight loss

Secher, A., Jelsing, J., Baquero, A. F., Hecksher-Sørensen, J., Cowley, M. A., Dalbøge, L. S., Hansen, G., Grove, K. L., Pyke, C., Raun, K., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci75276 · Cited by 961

Glucagon-Like Peptide-1 and Its Class B G Protein–Coupled Receptors: A Long March to Therapeutic Successes

Graaf, C. D., Donnelly, D., Wootten, D., Lau, J., Sexton, P. M., Miller, L. J., Ahn, J.-M., Liao, J., Fletcher, M. M., Yang, D., et al. (2016) · Pharmacological Reviews · doi:10.1124/pr.115.011395 · Cited by 403

Biased Receptor Signaling in Drug Discovery

Kenakin, T. (2019) · Pharmacological Reviews · doi:10.1124/pr.118.016790 · Cited by 321

Targeting GLP-1 receptor trafficking to improve agonist efficacy

Jones, B. J., Buenaventura, T., Kanda, N., CHABOSSEAU, P. L., Owen, B. M., Scott, R., Goldin, R. D., Angkathunyakul, N., Junior, I. R. C., Bosco, D., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03941-2 · Cited by 274

The role of glucagon‐like peptide 1 (GLP‐1) in addictive disorders

Klausen, M. K., Thomsen, M., Wortwein, G., & Fink‐Jensen, A. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15677 · Cited by 259

Discovery of Human Signaling Systems: Pairing Peptides to G Protein-Coupled Receptors

Foster, S. R., Hauser, A. S., Vedel, L., Strachan, R. T., Huang, X., Gavin, A. C., Shah, S. D., Nayak, A. P., Haugaard‐Kedström, L. M., Penn, R. B., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.010 · Cited by 253

GLP-1: Molecular mechanisms and outcomes of a complex signaling system

Smith, N. K., Hackett, T. A., Galli, A., & Flynn, C. R. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.04.010 · Cited by 204

Targeted delivery of antisense oligonucleotides to pancreatic β-cells

Ämmälä, C., Drury, W. J., Knerr, L., Ahlstedt, I., Stillemark-Billton, P., Huldt, C. W., Andersson, E.-M., Valeur, E., Jansson‐Löfmark, R., Janzén, D. L. I., et al. (2018) · Science Advances · doi:10.1126/sciadv.aat3386 · Cited by 191

GLP-1 and GIP receptor signaling in beta cells – A review of receptor interactions and co-stimulation

Mayendraraj, A., ROSENKILDE, M. M., & Gasbjerg, L. S. (2022) · Peptides · doi:10.1016/j.peptides.2022.170749 · Cited by 165

Super-resolution microscopy compatible fluorescent probes reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics

Ast, J., Arvaniti, A., Fine, N. H. F., Nasteska, D., Ashford, F. B., Stamataki, Z., Kőszegi, Z., Bacon, A., Jones, B. J., Lucey, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14309-w · Cited by 141

The Interplay of Glucagon-Like Peptide-1 Receptor Trafficking and Signalling in Pancreatic Beta Cells

Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121

GLP-1 and GLP-2 Orchestrate Intestine Integrity, Gut Microbiota, and Immune System Crosstalk

Abdalqadir, N., & Adeli, K. (2022) · Microorganisms · doi:10.3390/microorganisms10102061 · Cited by 119

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

Allostery and biased agonism at class B G protein-coupled receptors

Wootten, D., Miller, L. J., Koole, C., Christopoulos, A., & Sexton, P. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00049 · Cited by 112

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

GLP-1 and Exendin-4 Transiently Enhance GABAA Receptor–Mediated Synaptic and Tonic Currents in Rat Hippocampal CA3 Pyramidal Neurons

Korol, S. V., Jin, Z., Babateen, O., & Birnir, B. (2015) · Diabetes · doi:10.2337/db14-0668 · Cited by 101

Human GIP(3-30)NH2 inhibits G protein-dependent as well as G protein-independent signaling and is selective for the GIP receptor with high-affinity binding to primate but not rodent GIP receptors

Gabe, M. B. N., Sparre‐Ulrich, A. H., Pedersen, M. F., Gasbjerg, L. S., Inoue, A., Bräuner‐Osborne, H., Hartmann, B., & ROSENKILDE, M. M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.040 · Cited by 95

Genetic and biased agonist-mediated reductions in β-arrestin recruitment prolong cAMP signaling at glucagon family receptors

Jones, B. J., McGlone, E. R., Fang, Z., Pickford, P., Junior, I. R. C., Oishi, A., Jockers, R., Inoue, A., Kumar, S., Görlitz, F., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016334 · Cited by 98

Control of insulin secretion by GLP-1

Jones, B. J., Bloom, S. R., Buenaventura, T., Tomás, A., & Rutter, G. A. (2018) · Peptides · doi:10.1016/j.peptides.2017.12.013 · Cited by 99

Agonist-induced membrane nanodomain clustering drives GLP-1 receptor responses in pancreatic beta cells

Buenaventura, T., Bitsi, S., Laughlin, W. E., Burgoyne, T., Lyu, Z., Oqua, A. I., Norman, H., McGlone, E. R., Klymchenko, A. S., Junior, I. R. C., et al. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000097 · Cited by 96

Exendin-4 protects adipose-derived mesenchymal stem cells from apoptosis induced by hydrogen peroxide through the PI3K/Akt–Sfrp2 pathways

Zhou, H., Yang, J., Xin, T., Li, D., Guo, J., Hu, S., Zhou, S., Zhang, T., Zhang, Y., Han, T., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.033 · Cited by 81

Glucagon Like Peptide 1 Receptor Agonists for Targeted Delivery of Antisense Oligonucleotides to Pancreatic Beta Cell

Knerr, L., Prakash, T. P., Lee, R. G., Drury, W. J., Nikan, M., Fu, W., PIRIE, E. C., Maria, L. D., Valeur, E., Hayen, A., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c12043 · Cited by 80

Activation of glucagon‐like peptide‐1 receptors in the nucleus accumbens attenuates cocaine seeking in rats

Hernandez, N. S., O’Donovan, B., Ortinski, P. I., & Schmidt, H. D. (2017) · Addiction Biology · doi:10.1111/adb.12583 · Cited by 83

Biased agonism of clinically approved μ-opioid receptor agonists and TRV130 is not controlled by binding and signaling kinetics

Pedersen, M. F., Wróbel, T. M., Märcher-Rørsted, E., Pedersen, D. S., Møller, T. C., Gabriele, F., Pedersen, H., Matosiuk, D., Foster, S. R., Bouvier, M., et al. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107718 · Cited by 79

Chronic hyperglycemia downregulates GLP-1 receptor signaling in pancreatic β-cells via protein kinase A

Rajan, S., Dickson, L. M., Mathew, E., Orr, C. M. O., Ellenbroek, J. H., Philipson, L. H., & Wicksteed, B. L. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.01.010 · Cited by 79

Functional Consequences of Glucagon-like Peptide-1 Receptor Cross-talk and Trafficking

Roed, S. N., Nøhr, A. C., Wismann, P., Iversen, H. K., Bräuner‐Osborne, H., Knudsen, S. M., & Waldhoer, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592436 · Cited by 77

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

Ligand Residence Time at G-protein–Coupled Receptors—Why We Should Take Our Time To Study It

Hoffmann, C., Castro, M., Rinken, A., Leurs, R., Hill, S. J., & Vischer, H. F. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.099671 · Cited by 72

Overcoming the challenges of tissue delivery for oligonucleotide therapeutics

Gökirmak, T., Nikan, M., Wiechmann, S., Prakash, T. P., Tanowitz, M., & Seth, P. P. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.04.010 · Cited by 73

Central GLP-1 receptors: Novel molecular targets for cocaine use disorder

Hernandez, N. S., & Schmidt, H. D. (2019) · Physiology & Behavior · doi:10.1016/j.physbeh.2019.03.026 · Cited by 66

The postprandial actions of GLP-1 receptor agonists: The missing link for cardiovascular and kidney protection in type 2 diabetes

Thomas, M. C., Coughlan, M. T., & Cooper, M. E. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.004 · Cited by 63

The incretin hormone glucagon‐like peptide 1 increases mitral cell excitability by decreasing conductance of a voltage‐dependent potassium channel

Thiebaud, N., Llewellyn‐Smith, I. J., Gribble, F. M., Reimann, F. M., Trapp, S., & Fadool, D. A. (2016) · The Journal of Physiology · doi:10.1113/jp272322 · Cited by 60

Enhanced agonist residence time, internalization rate and signalling of the GIP receptor variant [E354Q] facilitate receptor desensitization and long‐term impairment of the GIP system

Gabe, M. B. N., van der Velden, W. J. C., Gadgaard, S., Smit, F. X., Hartmann, B., Bräuner‐Osborne, H., & ROSENKILDE, M. M. (2019) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13289 · Cited by 55

Characterization of genetic variants of GIPR reveals a contribution of β-arrestin to metabolic phenotypes

Kizilkaya, H. S., Sørensen, K. V., Madsen, J. S., Lindquist, P., Douros, J. D., Bork‐Jensen, J., Berghella, A., Gerlach, P. A., Gasbjerg, L. S., Mokrosiński, J., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01061-4 · Cited by 57

Rate of Homologous Desensitization and Internalization of the GLP-1 Receptor

Shaaban, G., Oriowo, M. A., & Al‐Sabah, S. (2016) · Molecules · doi:10.3390/molecules22010022 · Cited by 52

How Carvedilol activates β2-adrenoceptors

Benkel, T., Zimmermann, M., Zeiner, J., Bravo, S., Merten, N., Lim, V., Matthees, E. S. F., Drube, J., Miess, E., Malan, D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34765-w · Cited by 52

The endocrine disrupting potential of monosodium glutamate (MSG) on secretion of the glucagon-like peptide-1 (GLP-1) gut hormone and GLP-1 receptor interaction

Shannon, M., Green, B., Willars, G. B., Wilson, J., Matthews, N., Lamb, J., Gillespie, A. L., & Connolly, L. (2016) · Toxicology Letters · doi:10.1016/j.toxlet.2016.11.015 · Cited by 54

Signalling, trafficking and glucoregulatory properties of glucagon‐like peptide‐1 receptor agonists exendin‐4 and lixisenatide

Pickford, P., Lucey, M., Fang, Z., Bitsi, S., de la Serna, J. B., Broichhagen, J., Hodson, D. J., MINNION, J. S., Rutter, G. A., Bloom, S. R., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15134 · Cited by 49

Dissecting the roles of GRK2 and GRK3 in μ-opioid receptor internalization and β-arrestin2 recruitment using CRISPR/Cas9-edited HEK293 cells

Møller, T. C., Pedersen, M. F., van Senten, J. R., Seiersen, S. D., Mathiesen, J. M., Bouvier, M., & Bräuner‐Osborne, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-73674-0 · Cited by 50

Glucagon-like peptide-1 receptor internalisation controls spatiotemporal signalling mediated by biased agonists

Fletcher, M. M., Halls, M. L., Zhao, P., Clydesdale, L., Christopoulos, A., Sexton, P. M., & Wootten, D. L. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.003 · Cited by 49

Interrogating surface versus intracellular transmembrane receptor populations using cell-impermeable SNAP-tag substrates

Poc, P., Gutzeit, V. A., Ast, J., Lee, J., Jones, B. J., D’Este, E., Mathes, B., Lehmann, M., Hodson, D. J., Levitz, J., et al. (2020) · Chemical Science · doi:10.1039/d0sc02794d · Cited by 47

A Targeted RNAi Screen Identifies Endocytic Trafficking Factors That Control GLP-1 Receptor Signaling in Pancreatic β-Cells

Buenaventura, T., Kanda, N., Douzenis, P. C., Jones, B. J., Bloom, S. R., CHABOSSEAU, P. L., Junior, I. R. C., Bosco, D., Piemonti, L., Marchetti, P., et al. (2017) · Diabetes · doi:10.2337/db17-0639 · Cited by 45

Ligand-Specific Factors Influencing GLP-1 Receptor Post-Endocytic Trafficking and Degradation in Pancreatic Beta Cells

Fang, Z., Chen, S., Manchanda, Y., Bitsi, S., Pickford, P., David, A., Shchepinova, M. M., Junior, I. R. C., Hodson, D. J., Broichhagen, J., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218404 · Cited by 44

New Developments in Pharmacological Treatment of Obesity and Type 2 Diabetes—Beyond and within GLP-1 Receptor Agonists

Sztanek, F., Tóth, L. I., Pető, A., Hernyák, M., Diószegi, Á., & Harangi, M. (2024) · Biomedicines · doi:10.3390/biomedicines12061320 · Cited by 47

Biased action of the CXCR4-targeting drug plerixafor is essential for its superior hematopoietic stem cell mobilization

Jørgensen, A. S., Daugvilaite, V., Filippo, K. D., Berg, C., Mavri, M., Benned‐Jensen, T., Juzenaite, G., Hjortø, G. M., Rankin, S. M., Våbenø, J., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02070-9 · Cited by 43

GLP-1R Signaling and Functional Molecules in Incretin Therapy

Wan, W., Qin, Q., Xie, L., Zhang, H., Wu, F., Stevens, R. C., & Liu, Y. (2023) · Molecules · doi:10.3390/molecules28020751 · Cited by 44

Anti-Inflammatory Effects of GLP-1R Activation in the Retina

Puddu, A., & Maggi, D. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012428 · Cited by 42

The GPRC6A receptor displays constitutive internalization and sorting to the slow recycling pathway

Jacobsen, S. E., Ammendrup‐Johnsen, I., Jansen, A. M., Gether, U., Madsen, K. L., & Bräuner‐Osborne, H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762385 · Cited by 41

Live-cell reporters for fluorescence imaging

Junior, I. R. C. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2014.04.007 · Cited by 40

The complexity of signalling mediated by the glucagon-like peptide-1 receptor

Fletcher, M. M., Halls, M. L., Christopoulos, A., Sexton, P. M., & Wootten, D. L. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150244 · Cited by 40

Acylation of the Incretin Peptide Exendin-4 Directly Impacts Glucagon-Like Peptide-1 Receptor Signaling and Trafficking

Lucey, M., Ashik, T., Marzook, A., Wang, Y., Goulding, J., Oishi, A., Broichhagen, J., Hodson, D. J., MINNION, J. S., Elani, Y., et al. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.121.000270 · Cited by 37

The Influence of Peptide Context on Signaling and Trafficking of Glucagon-like Peptide-1 Receptor Biased Agonists

Fang, Z., Chen, S., Pickford, P., Broichhagen, J., Hodson, D. J., Corrêa, I. R., Kumar, S., Görlitz, F., Dunsby, C., French, P. M. W., et al. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00022 · Cited by 38

Pancreatic β‐cell imaging in humans: fiction or option?

Laurent, D., Vinet, L., Lamprianou, S., Daval, M., Filhoulaud, G., Ktorza, A., Wang, H., Sewing, S., Juretschke, H. P., Glombik, H., et al. (2015) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12544 · Cited by 37

GLP-1 Val8: A Biased GLP-1R Agonist with Altered Binding Kinetics and Impaired Release of Pancreatic Hormones in Rats

van der Velden, W. J. C., Smit, F. X., Christiansen, C. B., Møller, T. C., Hjortø, G. M., Larsen, O., Schiellerup, S. P., Bräuner‐Osborne, H., Holst, J. J., Hartmann, B., et al. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00193 · Cited by 38

The Novel GLP-1–Gastrin Dual Agonist ZP3022 Improves Glucose Homeostasis and Increases β-Cell Mass without Affecting Islet Number in db/db Mice

Dalbøge, L. S., Almholt, D. L. C., Neerup, T. S. R., Vrang, N., Jelsing, J., & Fosgerau, K. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.215293 · Cited by 35

Exploiting Covalent Chemical Labeling with Self-Labeling Proteins

Porzberg, N., Gries, K., & Johnsson, K. (2025) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030222-121016 · Cited by 41

Staphylococcus aureus–Derived PSMα Peptides Activate Neutrophil FPR2 but Lack the Ability to Mediate β-Arrestin Recruitment and Chemotaxis

Sundqvist, M., Christenson, K., Gabl, M., Holdfeldt, A., Jennbacken, K., Møller, T. C., Dahlgren, C., & Forsman, H. F. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900871 · Cited by 35

Glucagon-like peptide-1 receptors in nucleus accumbens, ventral hippocampus, and lateral septum reduce alcohol reinforcement in mice.

Allingbjerg, M.-L., Hansen, S. N., Secher, A., & Thomsen, M. (2022) · Experimental and Clinical Psychopharmacology · doi:10.1037/pha0000620 · Cited by 34

Uncovering CNS access of lipidated exendin-4 analogues by quantitative whole-brain 3D light sheet imaging

Skovbjerg, G., Roostalu, U., Salinas, C. G., Skytte, J. L., Perens, J., Clemmensen, C., Elster, L., Frich, C. K., Hansen, H. H., & Hecksher‐Sørensen, J. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109637 · Cited by 31

Revealing the tissue-level complexity of endogenous glucagon-like peptide-1 receptor expression and signaling

Ast, J., Nasteska, D., Fine, N. H. F., Nieves, D. J., Kőszegi, Z., Lanoiselée, Y., Cuozzo, F., Viloria, K., Bacon, A., Luu, N. T., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35716-1 · Cited by 33

The pro-healing effect of exendin-4 on wounds produced by abrasion in normoglycemic mice

Bacci, S., Laurino, A., Manni, M. E., Landucci, E., Musilli, C., Siena, G. D., Mocali, A., & Raimondi, L. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.06.056 · Cited by 33

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

Evaluation of biased agonism mediated by dual agonists of the GLP-1 and glucagon receptors

Darbalaei, S., Yuliantie, E., Dai, A., Chang, R., Zhao, P., Yang, D., Wang, M.-W., Sexton, P. M., & Wootten, D. L. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114150 · Cited by 35

Covalent Self-Labeling of Tagged Proteins with Chemical Fluorescent Dyes in BY-2 Cells and Arabidopsis Seedlings

Iwatate, R. J., Yoshinari, A., Yagi, N., Grzybowski, M., Ogasawara, H., Kamiya, M., Komatsu, T., Taki, M., Yamaguchi, S., Frommer, W. B., et al. (2020) · The Plant Cell · doi:10.1105/tpc.20.00439 · Cited by 33

Calcium-Sensing Receptor Internalization Is β-Arrestin–Dependent and Modulated by Allosteric Ligands

Mos, I., Jacobsen, S. E., Foster, S. R., & Bräuner‐Osborne, H. (2019) · Molecular Pharmacology · doi:10.1124/mol.119.116772 · Cited by 32

Barbadin selectively modulates FPR2-mediated neutrophil functions independent of receptor endocytosis

Sundqvist, M., Holdfeldt, A., Wright, S. C., Møller, T. C., Siaw, E., Jennbacken, K., Franzyk, H., Bouvier, M., Dahlgren, C., & Forsman, H. F. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118849 · Cited by 32

Internalization and desensitization of the human glucose-dependent-insulinotropic receptor is affected by N-terminal acetylation of the agonist

Ismail, S., Dubois-Vedrenne, I., Laval, M., Tikhonova, I. G., D’Angelo, R., Sanchez, C., Clerc, P., Ghérardi, M.-J., Gigoux, V., Magnan, R., et al. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.07.001 · Cited by 31

Exenatide inhibits necrosis by enhancing angiogenesis and ameliorating ischemia/reperfusion injury in a random skin flap rat model

He, J., Ma, X., Li, W., Liu, Y., & Lin, D. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107192 · Cited by 30

Conditional and Reversible Activation of Class A and B G Protein-Coupled Receptors Using Tethered Pharmacology

Podewin, T., Ast, J., Broichhagen, J., Fine, N. H. F., Nasteska, D., Leippe, P., Gailer, M., Buenaventura, T., Kanda, N., Jones, B. J., et al. (2018) · ACS Central Science · doi:10.1021/acscentsci.7b00237 · Cited by 32

Conjugation with glucagon like peptide-1 enables targeted protein degradation

Zhu, L., Zhou, Y., Zhang, B., Luo, Y., Chen, F., Yan, X., Cai, Y., Jiang, L., & Ge, J. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106908 · Cited by 30

Pancreatic alpha cells in diabetic rats express active GLP-1 receptor: Endosomal co-localization of GLP-1/GLP-1R complex functioning through intra-islet paracrine mechanism

Nakashima, K., Kaneto, H., Shimoda, M., Kimura, T., & Kaku, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-21751-w · Cited by 28

Distinct regions in the C-Terminus required for GLP-1R cell surface expression, activity and internalisation

Thompson, A., & Kanamarlapudi, V. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.06.012 · Cited by 27

A cAMP Biosensor-Based High-Throughput Screening Assay for Identification of Gs-Coupled GPCR Ligands and Phosphodiesterase Inhibitors

Vedel, L., Bräuner‐Osborne, H., & Mathiesen, J. M. (2015) · SLAS DISCOVERY · doi:10.1177/1087057115580019 · Cited by 26

Optimising cardioprotection during myocardial ischaemia: targeting potential intracellular pathways with glucagon-like peptide-1

Clarke, S. J., McCormick, L. M., & Dutka, D. P. (2014) · Cardiovascular Diabetology · doi:10.1186/1475-2840-13-12 · Cited by 25

Exendin-4 inhibits glioma cell migration, invasion and epithelial-to-mesenchymal transition through GLP-1R/sirt3 pathway

Nie, Z.-J., Zhang, Y., Chang, Y., Li, Q., & Zhang, Y.-L. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.092 · Cited by 25

Effects on pancreatic Beta and other Islet cells of the glucose-dependent insulinotropic polypeptide

Khan, R., Tomas, A., & Rutter, G. A. (2020) · Peptides · doi:10.1016/j.peptides.2019.170201 · Cited by 24

Molecular Pharmacology of the Incretin Receptors

Al‐Sabah, S. (2015) · Medical Principles and Practice · doi:10.1159/000433437 · Cited by 22

Differences in acute anorectic effects of long-acting GLP-1 receptor agonists in rats

Sisley, S. R., Smith, K., Sandoval, D. A., & Seeley, R. J. (2014) · Peptides · doi:10.1016/j.peptides.2014.05.008 · Cited by 21

Reconstitution of morphogen shuttling circuits

Zhu, R., Santat, L. A., Markson, J. S., Nandagopal, N., Gregrowicz, J., & Elowitz, M. B. (2023) · Science Advances · doi:10.1126/sciadv.adf9336 · Cited by 21

Detailed In Vitro Pharmacological Characterization of Clinically Tested Negative Allosteric Modulators of the Metabotropic Glutamate Receptor 5

Arsova, A., Møller, T. C., Vedel, L., Hansen, J. L., Foster, S. R., Gregory, K. J., & Bräuner‐Osborne, H. (2020) · Molecular Pharmacology · doi:10.1124/mol.119.119032 · Cited by 20

Spatiotemporal control of GLP-1 receptor activity

Manchanda, Y., Bitsi, S., Kang, Y., Jones, B. J., & Tomás, A. (2020) · Current Opinion in Endocrine and Metabolic Research · doi:10.1016/j.coemr.2020.07.003 · Cited by 21

Partial agonism improves the anti-hyperglycaemic efficacy of an oxyntomodulin-derived GLP-1R/GCGR co-agonist

Pickford, P., Lucey, M., Rujan, R., McGlone, E. R., Bitsi, S., Ashford, F. B., Junior, I. R. C., Hodson, D. J., Tomás, A., Deganutti, G., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101242 · Cited by 21

Molecular Characterisation of Small Molecule Agonists Effect on the Human Glucagon Like Peptide-1 Receptor Internalisation

Thompson, A., Stephens, J. W., Bain, S. C., & Kanamarlapudi, V. (2016) · PLOS ONE · doi:10.1371/journal.pone.0154229 · Cited by 19

Characterization of the real-time internalization of nine GPCRs reveals distinct dependence on arrestins and G proteins

Møller, T. C., Moo, E. V., Inoue, A., Pedersen, M. F., & Bräuner‐Osborne, H. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119584 · Cited by 19

Rapid, high efficiency isolation of pancreatic ß-cells

Clardy, S. M., Mohan, J. F., Vinegoni, C., Keliher, E. J., Iwamoto, Y., Benoist, C. O., Mathis, D. J., & Weissleder, R. (2015) · Scientific Reports · doi:10.1038/srep13681 · Cited by 18

Liraglutide modulates GABAergic signaling in rat hippocampal CA3 pyramidal neurons predominantly by presynaptic mechanism

Babateen, O., Korol, S. V., Jin, Z., Bhandage, A. K., Ahemaiti, A., & Birnir, B. (2017) · BMC Pharmacology and Toxicology · doi:10.1186/s40360-017-0191-0 · Cited by 19

Arrestin‐independent internalization of the GLP ‐1 receptor is facilitated by a GRK , clathrin, and caveolae‐dependent mechanism

Moo, E. V., Møller, T. C., Sørensen, F. A., Inoue, A., & Bräuner‐Osborne, H. (2025) · FEBS Journal · doi:10.1111/febs.17338 · Cited by 19

A Focus on Unusual ECL2 Interactions Yields β2‐Adrenergic Receptor Antagonists with Unprecedented Scaffolds

Scharf, M. M., Zimmermann, M., Wilhelm, F. M., Stroe, R., Waldhoer, M., & Kolb, P. (2020) · ChemMedChem · doi:10.1002/cmdc.201900715 · Cited by 18

Glucagon-like Peptide-1 Receptor (GLP-1R) Signaling: Making the Case for a Functionally Gs Protein-Selective GPCR

Lymperopoulos, A., Altsman, V. L., & Stoicovy, R. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157239 · Cited by 24

Proglucagon-derived peptides: human physiology and therapeutic potential

Gasbjerg, L. S., Nielsen, C. K., Suppli, M. P., Grøndahl, M. F. G., Holst, J. J., Knop, F. K., Jeppesen, P. B., & Lund, A. (2025) · Physiological Reviews · doi:10.1152/physrev.00057.2024 · Cited by 19

Beta cell specific probing with fluorescent exendin-4 is progressively reduced in type 2 diabetic mouse models

Lehtonen, J., Schäffer, L., Rasch, M. G., Hecksher‐Sørensen, J., & Ahnfelt‐Rønne, J. (2015) · Islets · doi:10.1080/19382014.2015.1137415 · Cited by 16

Targeted pH switched europium complexes monitoring receptor internalisation in living cells

Fradgley, J. D., Starck, M., Laget, M., Bourrier, E., Dupuis, E., Lamarque, L., Trinquet, E., Zwier, J. M., & Parker, D. (2021) · Chemical Communications · doi:10.1039/d1cc01029h · Cited by 17

A novel approach to treating opioid use disorders: Dual agonists of glucagon-like peptide-1 receptors and neuropeptide Y2 receptors

Merkel, R., Moreno, A., Zhang, Y., Herman, R. J., Nathan, J. B., Zeb, S., Rahematpura, S., Stecyk, K. S., Milliken, B. T., Hayes, M. R., et al. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.10.026 · Cited by 17

Localized GLP1 receptor pre-internalization directs pancreatic alpha cell to beta cell communication

Tong, J. C. L., Frazer-Morris, C., Shilleh, A. H., Viloria, K., de Bray, A., Nair, A. M., Johnson, P., Spiers, R. M., Kobiita, A., Olaniru, O. E., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.06.009 · Cited by 20

Emerging Role of Caveolin-1 in GLP-1 Action

Puddu, A., & Maggi, D. C. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.668012 · Cited by 16

Oleoylethanolamide modulates glucagon-like peptide-1 receptor agonist signaling and enhances exendin-4-mediated weight loss in obese mice

Brown, J. D., McAnally, D., Ayala, J. E., Burmeister, M. A., Morfa, C. J., Smith, L. H., & Ayala, J. E. (2018) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00459.2017 · Cited by 16

SNAP-tag-enabled super-resolution imaging reveals constitutive and agonist-dependent trafficking of GPR56 in pancreatic β-cells

Olaniru, O. E., Cheng, J., Ast, J., Arvaniti, A., Atanes, P., Huang, G. C., King, A., Jones, P. M., Broichhagen, J., Hodson, D. J., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101285 · Cited by 16

Resonance Energy Transfer-Based Approaches to Study GPCRs

Ayoub, M. A. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2015.10.008 · Cited by 19

Quantitative Impact of Plasma Clearance and Down-regulation on GLP-1 Receptor Molecular Imaging

Zhang, L., & Thurber, G. M. (2015) · Molecular Imaging and Biology · doi:10.1007/s11307-015-0880-2 · 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

229-LB: Quantification of GLP-1R Internalization and Recycling in Live ß Cells

Gray, S. M., Sloop, K. W., Ravn, P., Campbell, J. E., & D’Alessio, D. A. (2021) · Diabetes · doi:10.2337/db21-229-lb

Functional Consequences of Glucagon-like Peptide-1 Receptor Cross-talk and Trafficking

Roed, S. N., Nøhr, A. C., Wismann, P., Iversen, H. K., Bräuner‐Osborne, H., Knudsen, S. M., & Waldhoer, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592436 · Cited by 77

Ligand-Specific Factors Influencing GLP-1 Receptor Post-Endocytic Trafficking and Degradation in Pancreatic Beta Cells

Fang, Z., Chen, S., Manchanda, Y., Bitsi, S., Pickford, P., David, A., Shchepinova, M. M., Junior, I. R. C., Hodson, D. J., Broichhagen, J., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218404 · Cited by 44

The Interplay of Glucagon-Like Peptide-1 Receptor Trafficking and Signalling in Pancreatic Beta Cells

Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121

2114-P: Quantification of GLP-1R Trafficking in Primary Beta Cells in Response to Different Ligands

Gray, S. M., Ravn, P., Sloop, K. W., Campbell, J. E., & D’ALESSIO, J. (2020) · Diabetes · doi:10.2337/db20-2114-p