The Molecular Basis of G Protein–Coupled Receptor Activation

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637

High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

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The Energy Landscapes and Motions of Proteins

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Crystal structure of the β2 adrenergic receptor–Gs protein complex

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[19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors

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The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints

Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941

Dynamic personalities of proteins

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Crystal structure of the human β2 adrenergic G-protein-coupled receptor

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Structure of a nanobody-stabilized active state of the β2 adrenoceptor

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A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor.

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DeorphaNN: Virtual screening of GPCR peptide agonists using AlphaFold-predicted active-state complexes and deep learning embeddings

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Comparative Genomic Analysis Across Multiple Species to Identify Candidate Genes Associated with Important Traits in Chickens

Zhang, F., Chen, H., Chang, C. K., Zhou, J., & Zhang, H. (2025) · Genes · doi:10.3390/genes16060627 · Cited by 3

Cryo-EM structure of a cell-free synthesized full-length human β1-adrenergic receptor in complex with Gs

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C-Reactive Protein (CRP) Blocks the Desensitization of Agonistic Stimulated G Protein Coupled Receptors (GPCRs) in Neonatal Rat Cardiomyocytes

Wallukat, G., Mattecka, S., Wenzel, K., Schrödl, W., Vogt, B., Brunner, P., Sheriff, A., & Kunze, R. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11041058 · Cited by 3

Comparison of Experimental Approaches Used to Determine the Structure and Function of the Class D G Protein-Coupled Yeast α-Factor Receptor

Dumont, M. E., & Konopka, J. B. (2022) · Biomolecules · doi:10.3390/biom12060761 · Cited by 3

Basic Concepts of Design of Peptide-Based Therapeutics

Jois, S. D. S. (2022) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-031-04544-8_1 · Cited by 3

Analysis of the Function of Receptor Oligomers by Operational Models of Agonism

Giraldo, J., Zhou, B., Roche, D., Gil, C., Ortiz, J., Lans, I., Dalton, J. A. R., & Renault, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00012-8 · Cited by 3

Why medicines work

Swinney, D. C. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108175 · Cited by 3

Competition in drug binding and … the race to equilibrium

Vauquelin, G., & Maes, D. (2022) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12824 · Cited by 3

Versatile Fusion of Renown Pediculicidal Agents: An Innovative Thought

Naeem, D. A., & Shehzadi, A. (2021) · Haya The Saudi Journal of Life Sciences · doi:10.36348/sjls.2021.v06i03.001 · Cited by 3

Universal activation mechanism of class A GPCRsPreprint

Zhou, Q., Yang, D., Wu, M., Guo, Y., Guo, W., Li, Z., Cai, X., Dai, A., Shakhnovich, E. I., Liu, Z., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/710673 · Cited by 3

Single-molecule Dynamic In-Solution Inhibition Assay: A Method for Full Kinetic Profiling of Drug Candidate Binding to GPCRs in Native MembranesPreprint

Kaminski, T., Zhdanov, V. P., & Höök, F. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.16.460640 · Cited by 3

Universal mechanism of hormone and allosteric agonist mediated activation of glycoprotein hormone receptors as revealed by structures of follicle stimulating hormone receptorPreprint

Duan, J., Xu, P., Zhang, H., Luan, X., Yang, J., Mao, C., Shen, D., Ji, Y., He, X., Cheng, X., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.01.502312 · Cited by 3

Structure of the human Duffy antigen receptorPreprint

Saha, S., Khanppnavar, B., Maharana, J., Kim, H. R., Carino, C. M. C., Daly, C. A., Houston, S., Kumari, P., Yadav, P. N., Plouffe, B., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.09.548245 · Cited by 2

Structural Basis of GPCR-G Protein Pre-coupling and Activation: Insights from CCR1-Gi ComplexPreprint

Shao, Z., Dong, Y., Jia, R., Shen, Q., Yao, B., He, X., Yuan, Q., Shen, D.-D., Mao, C., Zhang, C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.01.621549 · Cited by 3

P-Rex1 Limits the Agonist-Induced Internalisation of GPCRs Independently of its Rac-GEF ActivityPreprint

Baker, M. J., Hampson, E., Islam, P., Moral, R. P., Maunders, E. A., Hornigold, K., Tsonou, E., Hornigold, D. C., Hubbard, R. E., Massey, A. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.14.648762 · Cited by 3

Impact of membrane lipid polyunsaturation on dopamine D2 receptor ligand binding and signaling

Jobin, M., Smedt, V. D., Ducrocq, F., Baccouch, R., Oummadi, A., Pedersen, M. H., Medel-Lacruz, B., Angelo, M.-F., Villette, S., Delft, P. V., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-022-01928-6 · Cited by 22

Identification of GNB1 as a downstream effector of the circRNA-0133711/miR-145-5p axis involved in breast cancer proliferation and metastasis

Zou, H., Chen, P., Li, Z., Yan, T., Cui, D., Gong, L., Fang, J., Ren, Y., Chen, M., Yu, J., et al. (2024) · ONCOLOGIE · doi:10.1515/oncologie-2024-0106 · Cited by 2

Key Interaction Changes Determine the Activation Process of Human Parathyroid Hormone Type 1 Receptor

Zhang, Y., Zheng, Q., Warshel, A., & Bai, C. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c15025 · Cited by 2

AGS3-based optogenetic GDI induces GPCR-independent Gβγ signalling and macrophage migration

Thotamune, W., Ubeysinghe, S., Rajarathna, C., Kankanamge, D., Olupothage, K., Chandu, A., Copits, B. A., & Karunarathne, A. (2025) · Open Biology · doi:10.1098/rsob.240181 · Cited by 2

Discovering Key Activation Hotspots in the M2 Muscarinic Receptor

Sugiura, Y., Ikuta, T., Sumii, Y., Tsujimoto, H., Suzuki, K., Suno, R., Ariff, P. N. A. M., Iwata, S., Shibata, N., Inoue, A., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c14385 · Cited by 2

GPCRchimeraDB: A Database of Chimeric G Protein-Coupled Receptors (GPCRs) to Assist Their Design

Crauwels, C., Díaz, A., & Vranken, W. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169164 · Cited by 2

Pharmacological Characterization of Dopamine Receptor DRD1 Variants and Exploration of Their Allosteric Activation

Wu, C., Wang, K., Liu, Z., Shen, S., Yang, Z., Shao, Z., & Yan, W. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00877 · Cited by 2

Molecular dynamics study of differential effects of serotonin-2A-receptor (5-HT2AR) modulators

Peeters, J., Bundel, D. D., & Vanommeslaeghe, K. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1013000 · Cited by 2

Increased cholesterol interactions in the active conformational state of the glucagon-like peptide-1 receptor

Naglekar, A., Chattopadhyay, A., & Sengupta, D. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.09.003 · Cited by 2

Glucose sensing and homeostasis by adipocyte GPCR

Hasan, N., & Chhabra, K. H. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1657747 · Cited by 3

P-Rex1 limits the agonist-induced internalization of GPCRs independently of its Rac-GEF activity

Baker, M. J., Hampson, E., Islam, P., Moral, R. P., Maunders, E. A., Hornigold, K., Tsonou, E., Malliri, A., Hornigold, D. C., Hubbard, R. E., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116403 · Cited by 7

Chemogenetic Activation of Oligodendrocytes Delays Postnatal Myelination by Promoting Progenitor Proliferation and Inhibiting Maturation

Cheli, V. T., Wartanian, T. P., González, D. A. S., Corral, J., Angeliu, C. G., Tumuluri, S. G., Wang, C., Smith, Z., & Paez, P. M. (2025) · Glia · doi:10.1002/glia.70094 · Cited by 2

The Allosteric Mechanism of G‐Protein‐Coupled Receptors is Induced Fit, Not Conformational Selection

Asadollahi, K., Gooley, P. R., & Weikl, T. R. (2025) · BioEssays · doi:10.1002/bies.70082 · Cited by 2

Extracellular nanobody screening using conformationally stable GPCR variants

Zhang, X., Gao, K., Nie, J., Meng, H., Sun, X., Zhao, J., & Liu, X. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2508879122 · Cited by 4

E 2 CB2former: Effecitve and Explainable Transformer for CB2 Receptor Ligand Activity Prediction

Xie, J., Ji, Y., Zeng, L., Xiao, X., Chen, G., Zhu, L., Mondal, J. J., & Chen, J. (2025) · International Joint Conference on Neural Networks (IJCNN) · doi:10.1109/ijcnn64981.2025.11227988 · Cited by 3

Dynamic Interaction: Synthetic Biology and Cell-Free Biosensors Drive Each Other Forward

Liu, S., Ma, B., Chi, H., Lu, Y., Abe, H., Wang, G., Guo, K., Jiang, C., Zhang, C., & Li, C. (2025) · ACS Nano · doi:10.1021/acsnano.5c12137 · Cited by 2

Elucidating the Structure and Activation Mechanisms of GPCRs Using Modern Computational and AI Tools

Uba, A. İ. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01977-y · Cited by 2

Mechanism of μ-opioid receptor inhibition by orphan GPR88

del Torrent, C. L., Raïch, I., Carrasco-Martinez, B., Lillo, J., Gallo, M., Andreu, D., Pardo, L., & Navarro, G. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2025.108084 · Cited by 2

Therapeutic antibodies targeting G protein-coupled receptors

Xu, Q., Huang, K., Shi, Y., Song, Y., Ying, T., & Yang, Z. (2026) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2025.12.004 · Cited by 4

A chemogenetic approach for temporal and cell-specific activation of endogenous GPCRs in vivo

Shingles, G., Pang, Q., Weng, J., Singer, R., Babar, W., Shen, J., Vazquez-Rivera, L., Chen, Y., Li, P., & Wang, W. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2501228123 · Cited by 2

Functional and structural insights into interactions between β-Arrestin 1 and Gαs or Gαi1

Duan, L., Kim, H., Suh, Y., Ahn, D., Kim, S., Hyun, J., Kwon, Y., Seong, J. Y., & Chung, K. Y. (2026) · Nature Communications · doi:10.1038/s41467-026-68690-z · Cited by 3

Tiny tools closing the gap: nanobodies in research and therapy

Abdellatif, M., Rajurkar, J., & Leonhardt, H. (2026) · Function · doi:10.1152/function.107.2025 · Cited by 2

In vivo functional profiling and structural characterization of the human GLP1R A316T variant

Eid, L. E., Manchanda, Y., Austin, G. O., Deane-Alder, K., Rujan, R., Mariam, Z., Oqua, A. I., Belousoff, M. J., de la Serna, J. B., Sloop, K. W., et al. (2026) · Science Advances · doi:10.1126/sciadv.adw0899 · Cited by 5

A catalogue of early diverged contemporary human genome variation reveals distinct Khoe-San populations

Jaratlerdsiri, W., Soh, P. X. Y., Gong, T., Jiang, J., Simayi, Z., Petersen, D. C., Holland, E., Chan, E. K. F., Theron, K. E., Haacke, W., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69269-4 · Cited by 2

A heteromeric TRP channel that functions as a WNT-activated G protein-coupled receptor

Hardy, E. P., Haider, A. N., Patel, M. M., Nesin, V., Hoang, H., Gostynska, S. E., Berry, W. L., Pioszak, A. A., Ahmad, M., Parnell, S. C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69932-w · Cited by 3

GPR146 in adipose tissue drives adipose-liver crosstalk and promotes hepatic steatosis in mice

Shi, Y., Cheng, K. Y., Thi, T. T., Wang, Y., Yang, Y., Cao, X., Chhay, V., Shen, Y., He, Y., Zhao, T., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70136-5 · Cited by 2

Microglial Neurotransmitter Receptors in Health and Disease

Bi, Q., Guo, C., Chen, N., Zhou, X., Zhou, Q., Liu, X., Shen, X. Z., & Shi, P. D. (2026) · Physiology · doi:10.1152/physiol.00030.2025 · Cited by 3

Single-position ligand modifications tune CB 2 R activity by targeting the toggle switch

Ganzoni, R. L. Z., Kosar, M., Han, Y., Vitale, R. M., Amodeo, P., Li, X., Zha, Z., Patej, K. J., Kicin, B., Strunden, T., et al. (2026) · Chemical Science · doi:10.1039/d6sc00062b · Cited by 2

The role of prostanoids in the retina and optic nerve in health and disease

Ward, E. L., Karnam, S., Changavi, A., Kumar, M., Maurya, S., Margeta, M. A., Sivak, J. M., Gronert, K., & Flanagan, J. G. (2026) · Progress in retinal and eye research · doi:10.1016/j.preteyeres.2026.101460 · Cited by 2

Wnt-dependent Frizzled clustering is required for Dishevelled phosphorylation but insufficient for β-catenin stabilization

Moldaver, S., Thibeault, P. E., Robitaille, M., Au, A., Lin, S., MacLeod, G. D. A. H., Junge, H. J., Gammons, M. V. R., Yip, C. M., & Angers, S. (2026) · Science Signaling · doi:10.1126/scisignal.aec0204 · Cited by 2

Metabolite sensing receptors in macrophage reprogramming: from inflammation to resolution

Rai, S. K., Gupta, S., & Sarangi, P. P. (2026) · Inflammation Research · doi:10.1007/s00011-026-02240-7 · Cited by 3

Molecular mechanisms of native ligand selectivity in catecholamine G protein-coupled receptors

Kahlous, N. A., Rinne, M. K., Xin, Z. C. Z., Li, Y., Chen, Y., Motso, A., Gao, K., Bergqvist, C., Sheng, H., Wáng, Y., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71361-8 · Cited by 2

Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin

Stadler, A. M., Granzin, J., Cousin, A., & Batra, R. (2020) · Scientific Reports · doi:10.1038/s41598-020-67944-0 · Cited by 2

Functional Modulation of Receptor Proteins on Cellular Interface with Optogenetic System

Endo, M., & Ozawa, T. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-8763-4_15 · Cited by 2

G-Protein Coupled Hormone Receptors of the Hypothalamic-Pituitary-Gonadal Axis are Targets of Endocrine Disrupting Chemicals

Suteau, V., Rodien, P., & Munier, M. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.96240 · Cited by 2

The therapeutic potential of targeting cardiac RGS4

Calvo, G. D., Lopez, T. B., & Lymperopoulos, A. (2023) · Therapeutic Advances in Cardiovascular Disease · doi:10.1177/17539447231199350 · Cited by 2

Confined modes of single-particle trajectories induced by stochastic resetting

Stanislavsky, A. A., & Weron, A. (2023) · Physical review. E · doi:10.1103/physreve.108.044130 · Cited by 2

From G-protein-coupled receptors to solute carriers—mass spectrometry informs dynamics, function, and regulation

Tang, H., & Robinson, C. V. (2024) · Chem · doi:10.1016/j.chempr.2024.02.022 · Cited by 2

Virtual screening, molecular docking and dynamics simulation studies to identify potential agonists of orphan receptor GPR78 targeting CNS disorders

Garisetti, V., Varughese, R. E., Anandamurthy, A., Haribabu, J., Garrote, C. A., & Gayathri, D. (2024) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2024.2405488 · Cited by 2

Characterization and phylogenetic analysis of vomeronasal receptors in the female muskrat (Ondatra zibethicus).

Chen, M.-Q., Zhu, B., Xie, W., Liu, Y.-N., Zhang, H.-L., & Weng, Q. (2024) · Gene · doi:10.1016/j.gene.2024.148998 · Cited by 1

Machine learning and deep learning based scoring functions in deciphering ligand-receptor binding: An application in drug design for GPCRs

Niu, T., Wang, N. X., & Wang, J. (2024) · Annual reports in computational chemistry · doi:10.1016/bs.arcc.2024.10.001 · Cited by 2

Unraveling GPCRs Allosteric Modulation. Cannabinoid 1 Receptor as a Case Study

Cruz, A., & Warshel, A. (2024) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26762 · Cited by 2

Molecular Glues: A New Approach to Modulating GPCR Signaling Bias

Kushnir, J., & Gumpper, R. H. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00734 · Cited by 2

Ligand specificity in Saccaromices cerevisiae G-Protein coupled receptor binding site design

Rienzo, L. D., Miotto, M., Milanetti, E., & Ruocco, G. (2025) · The Philosophical Magazine A Journal of Theoretical Experimental and Applied Physics · doi:10.1080/14786435.2025.2469145 · Cited by 2

A bio. tools collection of online resources for GPCR research

Laasfeld, T., Wunsch, F., Apostolakou, A. E., García‐Recio, A., Pándy‐Szekeres, G., Filipek, S., Niv, M. Y., Selent, J., Gloriam, D. E. I., & Bermúdez, M. (2025) · British Journal of Pharmacology · doi:10.1111/bph.17461 · Cited by 2

State of the art indicators for imaging purinergic dynamics in vitro and in vivo

Li, Y., Zhang, L., Li, B., Li, Y., & Wu, Z. (2025) · Purinergic Signalling · doi:10.1007/s11302-025-10095-6 · Cited by 2

Membrane Protein Modulators in Neuroinflammation

Chen, L., Zou, Z., Dang, C., Wang, G., Zhu, T., & Liang, G. (2025) · Current Neuropharmacology · doi:10.2174/011570159x375716250701111204 · Cited by 2

Mapping signal transduction in bistable jumping spider rhodopsin 1

Costa, F., Telari, E., Moreno-Rodríguez, D., Meloni, S., Olsen, J. M. H., Giacomello, A., & Muccio, G. D. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.10.040 · Cited by 2

Epitope analysis of an anti-mouse CCR1 monoclonal antibody S15040E using flow cytometry

Okada, A., Suzuki, H., Arimori, T., Tanaka, T., Kaneko, M. K., & Kato, Y. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102265 · Cited by 2

The Biological and Clinical Relevance of G Protein-Coupled Receptors to the Outcomes of Hematopoietic Stem Cell Transplantation: A Systematized Review

Golay, H. G., Mlakar, S. J., Mlakar, V., Nava, T., & Ansari, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163889 · Cited by 2

Role of Cannabinoid Receptors in Psychological Disorder

Jha, A. N., & Patel, D. M. (2020) · Borneo Journal of Pharmacy · doi:10.33084/bjop.v3i4.1569 · Cited by 2

Allosteric modulation of tethered ligand-activated G protein-coupled receptors

Mirka, V. M., & Ramachandran, R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-819771-4.00002-6 · Cited by 2

The computational modeling of allosteric modulation of metabotropic glutamate receptors

Pérez‐Benito, L., del Torrent, C. L., Pardo, L., & Tresadern, G. (2020) · Advances in pharmacology · doi:10.1016/bs.apha.2020.02.004 · Cited by 2

Biosensors Monitor Ligand-Selective Effects at Kappa Opioid Receptors

Oberhauser, L., & Stoeber, M. (2021) · Handbook of experimental pharmacology · doi:10.1007/164_2020_427 · Cited by 2

Pattern Recognition Molecules

Land, W. G. (2020) · Springer eBooks · doi:10.1007/978-3-030-53868-2_2 · Cited by 2

GPCR’s and Endocrinology

Gorvin, C. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00020-7 · Cited by 2

G-protein tonic inhibition of calcium channels in pancreatic β-cells

Quiroz‐Acosta, T., Bermeo, K., Arenas, I., & Garcı́a, D. E. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00447.2022 · Cited by 2

Combined Computational and Structural Approach into Understanding the Role of Peptide Binding and Activation of Melanocortin Receptor 4

Zachmann, J., Kritsi, E., Tapeinou, A., Zoumpoulakis, P. G., Tselios, T. V., & Matsoukas, M. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01196 · Cited by 2

GTPγS Assay for Measuring Agonist-Induced Desensitization of Two Human Polymorphic Alpha2B-Adrenoceptor Variants

Borges, J. I., Carbone, A. M., Cora, N., Sizova, A., & Lymperopoulos, A. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2573-6_12 · Cited by 2

Structure and dynamics of dynorphin peptide and its receptorPreprint

Ferre, G., Czaplicki, G., Demange, P., & Milon, A. (2019) · arXiv (Cornell University) · doi:10.48550/arxiv.1906.11659 · Cited by 2

Seeing β-arrestin in action: The role of β-arrestins in Histamine 1 Receptor signalingPreprint

Pietraszewska‐Bogiel, A., & Goedhart, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/775049 · Cited by 2

G protein-coupled receptor signaling regulates ER-mitochondria contactsPreprint

Lim, Y., Cho, I., Rennke, H. G., & Cho, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.11.088815 · Cited by 2

Protein kinase A controls the hexosamine pathway by tuning the feedback inhibition of GFAT-1Preprint

Ruegenberg, S., Mayr, F. A. M. C., Miethe, S., Atanassov, I., Baumann, U., & Denzel, M. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.23.216424 · Cited by 2

Functional modulation of PTH1R activation and signalling by RAMP2Preprint

Nemec, K., Schihada, H., Kleinau, G., Zabel, U., Grushevskyi, E. O., Scheerer, P., Lohse, M. J., & Maiellaro, I. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.08.471790 · Cited by 2

Toward a first principles understanding of the activation and deactivation mechanisms of class A G-protein coupled receptors and voltage-gated cation channelsPreprint

Wan, H., & Pearlstein, R. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.29.486149 · Cited by 2

Modeling the Orthosteric Binding Site of the G Protein-Coupled Odorant Receptor OR5K1

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Suitable use of FRET-based Biosensors for Quantitative Detection of GPCR ActivationPreprint

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Hemp Microgreen Mineral Content, Cannabinoids, Total Phenolics, and Antioxidants

Schayot, C. (2021) · doi:10.31390/gradschool_theses.5464 · Cited by 2

Biased activation of the vasopressin V2 receptor probed by NMR, paramagnetic ligands, and molecular dynamics simulationsPreprint

Gaibelet, G., Fouillen, A., Riché, S., Orcel, H., Mendre, C., Kanso, A., Lanotte, R., Nguyen, J., Dimon, J., Urbach, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.06.543947 · Cited by 2

Structural basis for constitutive activation and CXCL1 recognition of human herpesvirus 8-encoded G protein-coupled receptor KSHV-GPCRPreprint

Liu, A., Liu, Y., del Torrent, C. L., Zhang, W., Pardo, L., & Ye, R. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.27.573477 · Cited by 2

In vivo functional profiling and structural characterisation of the human Glp1r A316T variantPreprint

Eid, L. E., Deane-Alder, K., Rujan, R., Mariam, Z., Oqua, A. I., Manchanda, Y., Belousoff, M. J., de la Serna, J. B., Sloop, K. W., Rutter, G. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.19.619191 · Cited by 2

Revealing Water-Mediated Activation Mechanisms in the Beta 1-Adrenergic Receptor via OneOPES-Enhanced Free Energy LandscapesPreprint

Aureli, S., Rizzi, V., Piasentin, N., & Gervasio, F. L. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.03.641221 · Cited by 2

Computational design of allosteric pathways reprograms ligand-selective GPCR signalingPreprint

Hijazi, M., Kéri, D., Oggier, A., Sengar, A., Agosto, M. A., Wensel, T. G., & Barth, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.13.670154 · Cited by 3

Binding of Natural Peptide Ligands to the Neuropeptide Y5 Receptor

Rudolf, S., Kaempf, K., Vu, O., Meiler, J., Beck‐Sickinger, A. G., & Coin, I. (2021) · Angewandte Chemie · doi:10.1002/ange.202108738 · Cited by 1

Structure Prediction, Evaluation, and Validation of GPR18 Lipid Receptor Using Free Programs

Michalik, I., Kuder, K., Kieć‐Kononowicz, K., & Handzlik, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147917 · Cited by 1

Design of Drug Efficacy Guided by Free Energy Simulations of the β 2 ‐Adrenoceptor

Panel, N., Vo, D. D., Kahlous, N. A., Hübner, H., Tiedt, S., Matricon, P. G., Pacalon, J., Fleetwood, O., Kampen, S., Luttens, A., et al. (2023) · Angewandte Chemie · doi:10.1002/ange.202218959 · Cited by 2

toGC: A pipeline to correct gene model for functional excavation of dark GPCRs in Phytophthora sojae

Qiu, M., Yan, C., Li, H., Zhao, H., Tu, S., Sun, Y., Yong, S., Wang, M., & Wang, Y. (2024) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2024.03.077 · Cited by 1

Identification of two critical amino acid residues in short-chain aldehyde-responsive odorant receptors

Kanemaki, R., Hayakawa, T., Kudo, H., Yohda, M., & Fukutani, Y. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae033 · Cited by 1

Dynamic mechanism for subtype selectivity of endocannabinoids

Dutta, S., Zhao, L., & Shukla, D. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111434 · Cited by 1

RGS Proteins in Sympathetic Nervous System Regulation: Focus on Adrenal RGS4

Lymperopoulos, A., & Stoicovy, R. A. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2910355 · Cited by 1

Unveiling the complexity of G protein-coupled receptor heteromers: advances in live cell imaging technologies and biochemical methods

Kim, H., Lee, H., & Seong, J. (2024) · Med-X · doi:10.1007/s44258-024-00029-z · Cited by 1

Biased Signaling in G Protein-Coupled Receptors: Understanding the Biological Relevance and Tools for Probing Functionally Selective Ligands

Fallon, B. S., Rondem, K. E., Mumby, E. J., & English, J. G. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00871 · Cited by 1

Reaction kinetics of membrane receptors: a spatial modeling approach

Cengiz, A., & Lawley, S. D. (2025) · Journal of Mathematical Biology · doi:10.1007/s00285-025-02217-w · Cited by 1

Molecular insights into the unique activation and allosteric modulation mechanisms of the human mas-related G-protein-coupled receptor X1

Wu, Z., Sun, X., Su, J., Zhang, X., & Li, C. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144815 · Cited by 1

Structural Basis for G Protein–Coupled Receptor Signaling

Erlandson, S. C., McMahon, C. T., & Kruse, A. C. (2018) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070317-032931 · Cited by 128

Structural mechanism of G protein activation by G protein-coupled receptor

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Active state structures of G protein-coupled receptors highlight the similarities and differences in the G protein and arrestin coupling interfaces

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G protein‐coupled receptors: a count of 1001 conformations

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Structural Aspects of GPCR-G Protein Coupling

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