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

Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935

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

Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,709

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

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Critical Residues in the Gβ Subunit Mediate Selective Recruitment of the Gαq Heterotrimer to Activated G Protein-Coupled Receptors

Yao, Y., Wang, D., Wang, S., Ouyang, X., Zhao, L., Chen, H., & Xu, J. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00167 · Cited by 1

Pharmacological characterization of vampire bat-derived CGRP at the human CGRP receptor in the Xenopus oocyte system

Carleer, K., Raval, K., Tudzarova, S., & Tytgat, J. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108466 · Cited by 1

Development of a HiBiT Peptide-Based NanoBRET Ligand Binding Assay for Galanin Receptor 1 in Live Cells

Zhu, H., Daly, H. C., Yang, T. G., Born, J. R., Camacho‐Hernandez, G. A., Yuan, M., Inglese, M., Chenniappan, V. K., Zimmerman, K., Hurst, R., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00166 · Cited by 1

The RhoGDIβ-Rac1-CARD9 Signaling Module Mediates Islet β-Cell Dysfunction Under Chronic Hyperglycemia

Kowluru, A., & Wang, J. (2025) · Cells · doi:10.3390/cells14141046 · Cited by 1

MARY1 restores mitochondrial homeostasis and accelerates renal recovery following acute kidney injury

Raj, P. V. S., Janda, J., Scholpa, N. E., Hurtado, K. A., & Schnellmann, R. G. (2025) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00232.2025 · Cited by 1

Computational discovery of natural medicines targeting adenosine receptors for metabolic diseases

Wang, P., Xu, Z., Deng, Y., Yuan, H., Wu, Y.-K., Jiang, J., Lyu, Z., & Li, Z. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1671415 · Cited by 1

Artificial intelligence in GPCR drug discovery: A paradigm shift in computational pharmacology

Vinter, A., & Grgičević, I. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00047-9 · Cited by 1

Monoclonal Antibody 5F1 Modulates Formyl Peptide Receptor 1 Conformation for Transmembrane Signaling

Wang, Y., Liu, Y., Chang, Y., & Ye, R. D. (2025) · FASEB BioAdvances · doi:10.1096/fba.2025-00145 · Cited by 1

KCTD Family: Emerging Regulators of GPCR Biased Signaling

Jiang, W., & Zheng, S. (2025) · Handbook of experimental pharmacology · doi:10.1007/164_2025_766 · Cited by 1

Vibrational energy landscapes and energy flow in GPCRs: comparison between class A and class B GPCRs using all atom and coarse-grained models

Poudel, H., Shaon, P. H., Wales, D. J., & Leitner, D. M. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp02918j · Cited by 1

Conformational Heterogeneity Underlying Divergent Signaling in Class A G Protein-Coupled Receptors

Georgiou, K., & Kolocouris, A. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00102 · Cited by 1

Light‐Based Molecular Tools to Precisely Monitor and Operate β‐Adrenoceptors

Ignazzitto, M. T., Gómez‐Santacana, X., Llebaria, A., & Rovira, X. (2025) · Medicinal Research Reviews · doi:10.1002/med.70018 · Cited by 1

Biotinylated RAFT Styrene/Maleic Acid Copolymers for Biosensor Applications of Membrane Proteins

Gomes, M. A. G. B., Glueck, D., Monjal, V., Damian, M., Guillet, P., Banères, J., Keller, S., & Durand, G. (2025) · ACS Applied Polymer Materials · doi:10.1021/acsapm.5c02955 · Cited by 1

Elucidating zerumbone’s low-efficacy agonism at the μ-opioid receptor via molecular dynamics simulation and Markov state modeling

Ayub, W. M. W., Marjohan, N. A., Khalid, M. H., Perimal, E. K., & Jamali, M. A. M. (2025) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-025-00677-2 · Cited by 1

Cannabidiol and Parkinson's disease: Investigating receptor interactions and their therapeutic implications

Okrah, E. A., Allan, C. Y., Doblin, M. S., & Annesley, S. J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108943 · Cited by 2

Investigating the Structural Basis of Diacetyl Recognition by the G‑Protein-Coupled Receptor ODR-10 in Caenorhabditis elegans

Rienzo, L. D., Milanetti, E., Folli, V., & Ruocco, G. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c04257 · Cited by 1

Computational modelling reveals novel insights into GnRH receptor activation and binding dynamics

Paspali, E., Ferro, V. A., Kubiak-Ossowska, K., & Mulheran, P. A. (2025) · Scientific Reports · doi:10.1038/s41598-025-26518-8 · Cited by 1

Prompt-based multimodal representation learning for drug repurposing

Liu, J., Kaicheng, U., Rana, D., Zhang, S. M., Yu, J., Yang, S., Jin, B., Wang, X., Yang, Z., Tang, H., et al. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf636 · Cited by 1

Structure-based design of macrocyclic peptides to generate functional antibodies against G protein-coupled receptors

Nepveu-Traversy, M.-É., Hassanzadeh, M., Bruneau‐Cossette, L., Besserer‐Offroy, É., Brouillette, R. L., Morissette, S., Traboulsi, H., Kirby, K., Murza, A., Longpré, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66030-1 · Cited by 1

G-protein-coupled receptor diversity and evolution in the closest living relatives of metazoaPreprint

Bayonas, A. G. D. L., & King, N. (2025) · eLife · doi:10.7554/elife.107467.4 · Cited by 3

Live cell luminescence-based Gαq-PLC-β interaction assay: Development and application at the serotonin 5-HT2A receptor

Pottie, E., & Stove, C. P. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108094 · Cited by 2

Investigating the Electrostatics Underlying Activation of the β2 Adrenergic Receptor

Montgomery, J. M., & Lemkul, J. A. (2026) · Biochimica et Biophysica Acta - Biomembranes · doi:10.1016/j.bbamem.2026.184503 · Cited by 1

The multifaceted roles of G protein-coupled receptor C3aR1 in disease: From immunomodulation to cancer progression

Cui, J., Shen, F., Zhang, C., Fu, C., Zhu, J., & Zhuang, T. (2026) · Pathology - Research and Practice · doi:10.1016/j.prp.2026.156386 · Cited by 1

Computational design of constitutively active mutants of Dopamine D2 receptor inspired by ligand-independent activation mechanisms

Chen, Y., Saarinen, M., Naraine, A. S., Carlsson, J., Svenningsson, P., & Delemotte, L. (2026) · BMC Biology · doi:10.1186/s12915-026-02542-6 · Cited by 1

Structural and dynamic insights into ligand recognition and activation of somatostatin receptor 3

Chen, X., Guo, S., Li, Y.-G., Liu, A.-K., Kuang, J., Shi, P., Yu, L., Yang, F., & Tian, C.-L. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01740-2 · Cited by 1

A Transferable and Robust Computational Framework for Class A GPCR Activation Free Energies

Aureli, S., Piasentin, N., Fröhlking, T., Rizzi, V., & Gervasio, F. L. (2026) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.5c03834 · Cited by 1

Rare variant in intracellular loop-2 alters the spatial distribution and transducer coupling selectivity of the ghrelin receptor

Balfe, E. M., Torbey, A. G., Stępniewski, T. M., Zhou, Y., Kohlenbach, L., Sency, J. A., Inoue, A., Slosky, L. M., Selent, J., Barak, L. S., et al. (2026) · Molecular Pharmacology · doi:10.1016/j.molpha.2026.100119 · Cited by 1

Lactylation-related gene signature for prognosis prediction and immune infiltration assessment in lung adenocarcinoma via bulk and single-cell RNA sequencing

Zhou, H., Liu, W., Liu, Z., & Lan, Y. (2026) · Discover Oncology · doi:10.1007/s12672-026-04845-0 · Cited by 1

Lactobacillus paragasseri LPG-9 reduces placental inflammation in intrahepatic cholestasis of pregnancy by regulating TGR5 in mice

Huang, W., Zhang, J., Shan, J., Shen, W., Du, P., Liu, J., Guo, X., Chen, Z., Zeng, W., Lin, Q., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-09869-4 · Cited by 1

Dopamine D2 Receptor Isoform Heteroreceptor Complexes with the Growth Hormone Secretagogue Receptor 1a Reveals Isoform-Specific Interaction Interface Dynamics

Cáceres-Quezada, Á., Borroto‐Escuela, D. O., & Fierro, A. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c00308 · Cited by 1

Identification of Subtype-Selective Binding Sites in the Opioid Receptor Family

Gomes, A. A. S., Guillot, B., Jelsch, C., & Giraldo, J. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02403 · Cited by 1

Structural insights into subtype-specific agonist recognition by sphingosine-1-phosphate receptors

Yu, L., Jiao, H., Pang, B., Ti, R., Gan, B., Qin, Z., Wang, J., Zhu, L., Hu, H., & Ren, R. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003381 · Cited by 1

A Systematic Benchmark Study of Free Energy Methods for Quantifying Light-Responsive Binding Affinities of Photoswitchable Antagonists of Beta-Adrenergic Receptors

Khavani, M., Bakhtiiari, A., Khalvati, L., Leurs, R., & Liang, R. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03756 · Cited by 1

Phospholipid-chemoattractant pathways: new pharmacological targets for stratified treatment of immune-mediated diseases

Condorelli, G. A., Genova, R., Bonifacio, D., & Dragostin, O. M. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118005 · Cited by 1

Immunomodulatory crosstalk between GPCR and hippo signaling in cancer: implications for tumor immunity and therapeutic targeting

Ren, X., Xie, T., Liu, L., Jin, X., & Zhang, M. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1765361 · Cited by 1

Biophysical Sensing Tools in Drug Discovery: Integrating Kinetics, Thermodynamics, Cellular Target Engagement and Structure

Balıkçı, E., & Akıl, C. (2026) · Sensors · doi:10.3390/s26103105 · Cited by 2

Distinct pharmacological profile of a dopamine D3 receptor ligand with potential therapeutic effect in restless legs syndrome

Lai, Y., Keegan, B. M., Ciruela-Jardí, M., Cao, J. J., Hsieh, K., Earley, C. J., Shi, L., Moreno, E., Pardo, L., Newman, A. H., et al. (2026) · SLEEP · doi:10.1093/sleep/zsag134 · Cited by 1

Deciphering Infrared Difference Spectra of Bovine Rhodopsin in the Amide I Region by Localized Anharmonic Vibrational Calculations

松山, 奈., Katayama, K., & Yagi, K. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c01639 · Cited by 2

Making sense of subcellular H2O2 in mammals

Waldeck‐Weiermair, M., Covington, T. A., Pandey, A. K., & Michel, T. M. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100080 · Cited by 1

Oxylipin-mediated metabolic signatures of symbiosis homeostasis and thermal stress in a model sea anemone

Botana, M. T., Lewis, R. E., Mitchell, K. A., Salamin, O., Revol-Cavalier, J., Heit, E. M., Gamba, A. G., Wilkinson, S., Rosset, S. L., Oakley, C. A., et al. (2026) · The ISME Journal · doi:10.1093/ismejo/wrag143 · Cited by 1

Epitope Mapping of Anti-Mouse C-C Motif Chemokine Receptor 1 Monoclonal Antibodies Developed by the Cell-Based Immunization and Screening Method

Okada, A., Suzuki, H., Kaneko, M. K., & Kato, Y. (2026) · Monoclonal Antibodies in Immunodiagnosis and Immunotherapy · doi:10.1177/21679436261459606 · Cited by 1

Mitochondria-centered neuroenergetic dysfunction in treatment-resistant depression: A conceptual framework for multi-layer nutritional modulation and serum BDNF as a biomarker of systemic recovery

Zhang, R. H. (2026) · Nutritional Psychiatry · doi:10.1016/j.nupsyc.2026.100024

Visual arrestin-1: how did we learn what we know today about this protein?

Gurevich, V. V., & Gurevich, E. V. (2026) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2026.101491 · Cited by 1

G protein selectivity in group I metabotropic glutamate receptors

Lu, Y., Wen, T., Lu, X., Zhang, G., Meng, T., Liu, T., Wang, X., Shen, Y., & Yang, X. (2026) · Science Advances · doi:10.1126/sciadv.aee0044 · Cited by 1

Molecular Dynamics and Free Energy Calculations Predict Binding Mode and Affinity Determinants of Specialized Pro-Resolving Mediators at GPR101

Hasselstrøm, D. H., Awad, M., Hansen, T. V., & Gani, O. (2026) · ACS Omega · doi:10.1021/acsomega.5c13583 · Cited by 1

SSTR2 receptor states and cellular metabolism modulate 177Lu-DOTATATE binding affinity

Lundsten, S., Engbers, P. A. M., Nonnekens, J., & Bondza, S. (2026) · EANM Innovation · doi:10.1016/j.eanmi.2026.100288 · Cited by 1

Recent advances on structure and dynamics of G protein–coupled receptors using single-molecule Förster resonance energy transfer

Quast, R. B., & Margeat, E. (2026) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2026.103343 · Cited by 1

GPR19 Drives Cell Cycle Progression via ERK-Dependent FOXM1 Activation in p53-Mutant Breast Cancer

Qiu, J., Tian, C., Li, H., Gao, S., Yang, C., Luo, Q., Liu, Y., He, K., Li, K., Peng, Y., et al. (2026) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl52064 · Cited by 1

C5aR2 signaling mechanisms via the β-arrestin–dependent pathway observed in microsecond-scale molecular dynamics simulations

Dragan, P., & Latek, D. (2026) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2026.105028 · Cited by 1

Mechanism of GPR84 allosteric modulation at a helix 8–proximate site

Zhang, X., Guseinov, A.-A., Jenkins, L., Zhou, J., Gossen, F., Wang, P., Mahmud, Z. A., Li, Y., Mahardhika, A. B., Müller, C. E., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeh5849 · Cited by 1

Characterization of Critical Residues in the Extracellular and Transmembrane Domains of the Endothelin Type B Receptor for Propagation of the Endothelin-1 Signal

Doi, T., Kikuta, K., & Tani, K. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00158 · Cited by 1

Phosphodiesterase 4 mediates interleukin‐8‐induced heterologous desensitization of the β 2 ‐adrenergic receptor

Rich, T. C., Leavesley, S. J., Brandon, A. P., Evans, C. A., Raju, S. V., & Wagener, B. M. (2021) · The FASEB Journal · doi:10.1096/fj.202002712rr · Cited by 1

Agonists in the Extended Conformation Stabilize the Active State of β-Adrenoceptors

Efimov, A. V., Meshcheryakova, O. V., & Ryazanov, A. G. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922070057 · Cited by 1

Advances in the molecular level understanding of G-protein coupled receptor

Roy, A. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.07.013 · Cited by 1

Label-free LC-MS based assay to characterize small molecule compound binding to cells

Chen, M., Zhu, Z., Wisniewski, T., Zhang, X., McLaren, D. G., Weinglass, A. B., & Saldanha, S. A. (2022) · SLAS DISCOVERY · doi:10.1016/j.slasd.2022.08.005 · Cited by 1

Stickier G-protein conformations

Garcia‐Marcos, M. (2023) · Nature Chemical Biology · doi:10.1038/s41589-022-01239-5 · Cited by 1

Identifying highly effective fludarabine-based novel target cancer therapy agents by in silico studies

Yücel, K., & Azak, H. (2024) · Experimental Biomedical Research · doi:10.30714/j-ebr.2024.211 · Cited by 1

Transient motion classification and segment analysis of diffusive trajectories of G proteins and coupled-receptors in a living cell

Stanislavsky, A. A., & Weron, A. (2024) · Journal of Mathematics in Industry · doi:10.1186/s13362-024-00151-y · Cited by 1

Vitamin A supply in the eye and establishment of the visual cycle

Bandara, S., & Lintig, J. V. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.09.003 · Cited by 2

N-Branched Tricyclic Guanidines as Novel Melanocortin-3 Receptor Agonists and Melanocortin-4 Receptor Antagonists

Weirath, N. A., Zajac, J. W. P., Donow, H. M., Lavoi, T. M., Pinilla, C., Santos, R. G., Prajapati, R., Speth, R. C., Ericson, M. D., Sarupria, S., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01556 · Cited by 1

Mechanisms of sensing abiotic stress responses in plants

Sehgal, H., Pant, C., Ray, S., Sharma, N., & Joshi, M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-13490-6.00018-7 · Cited by 1

Artificial Intelligence and Machine Learning Approaches for Target-Based Drug Discovery: A Focus on GPCR-Ligand Interactions

Otun, M. (2025) · Journal of applied science and environmental management · doi:10.4314/jasem.v29i3.7 · Cited by 1

AMF30a promotes survival and function of human corneal endothelial cells by regulating TGF-β/ROCK/HIPPO pathway

Ryu, Y., Son, H.-J., Hwang, J. S., Noh, K. B., Oh, S., Choi, E., & Shin, Y. J. (2025) · Scientific Reports · doi:10.1038/s41598-025-13656-2 · Cited by 1

Gβγ Signaling: Lessons Across the Cellular Multiverse

Qayum, S., Pétrin, D., Tanny, J. C., & Hébert, T. E. (2025) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-062124-033726 · Cited by 1

GPCR Heterodimers: Implications for Biased Signaling

Li, L., Li, Y., Zhang, S., Shen, C., Meng, J., & Liu, J. (2025) · Handbook of experimental pharmacology · doi:10.1007/164_2025_762 · Cited by 1

Opioid Receptors and their complex mechanisms of action

Aneesha, D. (2024) · Journal of High School Science · doi:10.64336/001c.116672 · Cited by 1

Ligand binding represses bacterial histidine kinase activity by inhibiting its dimerization

Sankhe, G. D., Xing, J., Xiao, X., Buglino, J. A., Li, H., Zhulin, I. B., & Glickman, M. S. (2026) · FEBS Journal · doi:10.1111/febs.70621 · Cited by 1

Unsupervised Classification of G‑Protein Coupled Receptors and Their Conformational States Using IChem Intramolecular Interaction Patterns

Koensgen, F., Silva, F. D., Rognan, D., & Kellenberger, E. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00054 · Cited by 1

Targeting Orexin Neurons for Treatment of Obesity is It Feasible in Human Being-A Systematic Review

Kaur, K. K., Allahbadia, G. N., & Singh, M. (2019) · Journal of Neurology Research Review & Reports · doi:10.47363/jnrrr/2019(1)104 · Cited by 1

Allostery of atypical modulators at oligomeric G protein-coupled receptors

Shivnaraine, R. V., Kelly, B., Elmslie, G., Huang, X., Yue, D., Seidenberg, M., Wells, J. W., & Ellis, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-88399-x · Cited by 1

Platelet Activating Factor Receptor Binding and Contractile Protein Expression by Ovine Fetal Pulmonary Vascular Smooth Muscle Cells: Role in Rho Kinase Mediation of PAF Receptor-Linked Physiological Responses

Ibe, B. O., Douglass, A. M., Douglass, S. M., & Renteria, L. S. (2021) · Medical Research Archives · doi:10.18103/mra.v9i7.2460 · Cited by 1

Receptor–enzyme complex structures show how receptors start to switch off

Gurevich, V. V., & Gurevich, E. V. (2021) · Nature · doi:10.1038/d41586-021-01873-4 · Cited by 1

Squaring off with G protein-coupled receptors function in polymer nanoscale lipid bilayers

Soubias, O. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.09.013 · Cited by 1

Distinct antagonist-bound inactive states underlie the divergence in the structures of the dopamine D2 and D3 receptorsPreprint

Lane, J. R., Abramyan, A. M., Verma, R. K., Lim, H. D., Javitch, J. A., & Shi, L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/640870 · Cited by 1

Structural basis of bile acid receptor activation and Gs couplingPreprint

Yang, F., Mao, C., Guo, L., Lin, J., Ming, Q., Xiao, P., Wu, X. Y., Shen, Q., Guo, S., Shen, D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.24.104034 · Cited by 1

A Genetically Encoded Trimethylsilyl 1D 1 H-NMR Probe for Conformation Change in Large Membrane Protein ComplexesPreprint

Liu, Q., He, Q., Lyu, X., Yang, F., Zhu, Z., Xiao, P., Yang, Z., Zhang, F., Yang, Z.-Y., Wang, X.-Y., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.18.873729 · Cited by 1

Molecular insights into the μ-opioid receptor biased signalingPreprint

Cong, X., Maurel, D., Déméné, H., Vasiliauskaité-Brooks, I., Hagelberger, J., Peysson, F., Saint‐Paul, J., Golebiowski, J., Granier, S., & Sounier, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436421 · Cited by 1

Modelling altered signalling of G-protein coupled receptors in inflamed environment to advance drug designPreprint

Ray, S., Thies, A., Sunkara, V., Wulkow, H., Celik, M. Ö., Yergöz, F., Schütte, C., Stein, C., Weber, M., & Winkelmann, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.20.465073 · Cited by 1

Politics, administration, and national development

Kim, K.-U. (1971) · ScholarSpace (University of Hawaii at Manoa) · Cited by 1

G-Protein-Coupled Receptors

Wettschureck, N. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_70 · Cited by 1

G-Protein-Coupled Receptors

Wettschureck, N. (2020) · Springer eBooks · doi:10.1007/978-3-030-21573-6_70-1 · Cited by 1

Dynamic allosteric networks drive adenosine A 1 receptor activation and G-protein couplingPreprint

Maria‐Solano, M. A., & Choi, S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.08.502889 · Cited by 1

The Calcium‐Sensing Receptor ( CaSR ) in Disease

Keller, A. N., Josephs, T. M., Gregory, K. J., & Leach, K. (2022) · doi:10.1002/9781119564782.ch17 · Cited by 1

Ten Years of GPCR Structures

Hanson, M. A., & Orencia, M. C. (2022) · doi:10.1002/9781119564782.ch9 · Cited by 1

Cryo-EM structures of the human G-protein coupled receptor 1 (GPR1) – Gi protein complexes bound to the full-length chemerin and to its C-terminal nonapeptidePreprint

Liu, A., Liu, Y., Chen, G., Lyu, W., Ye, F., Wang, J., Liao, Q., Zhu, L., Du, Y., & Ye, R. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.03.543554 · Cited by 1

The discovery of small-molecule modulators for the ACKR3 receptor

Riemens, R. (2023) · doi:10.5463/thesis.270 · Cited by 1

Flipping the GPCR Switch: Structure–Based Development of Selective Cannabinoid Receptor 2 Inverse AgonistsPreprint

Carreira, E. M., Kosar, M., Sarott, R. C., Sykes, D. A., Viray, A. E. G., Vitale, R. M., Tomašević, N., Li, X., Ganzoni, R. L. Z., Kicin, B., et al. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-w3ggn · Cited by 1

Binding Position Dependent Modulation of Smoothened Activity by CyclopaminePreprint

Kim, K., Bansal, P. D., & Shukla, D. (2024) · bioRxiv · doi:10.1101/2024.02.08.579369 · Cited by 1

AGS3-based optogenetic GDI induces GPCR-independent Gβγ signaling and macrophage migrationPreprint

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From Mutations to Disease: Computational Analysis and Interpretation of GPCR-Associated PathogenicityPreprint

Velloso, J. P. L., de Sá, A. G. C., & Ascher, D. B. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.17.599437 · Cited by 1

Characterization of binding kinetics and intracellular signaling of new psychoactive substances targeting cannabinoid receptor using transition-based reweighting methodPreprint

Dutta, S., & Shukla, D. (2024) · eLife · doi:10.7554/elife.98798.1 · Cited by 1

A GPCR-G protein-β-arrestin megacomplex induced by an allosteric modulatorPreprint

He, G., Sun, Q., Xu, X., Kong, F., Zhang, S., Ye, K., Sun, X., Chen, X., Yan, C., & Liu, X. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.24.645131 · Cited by 1

Extracellular Nanobody Screening using Conformationally Stable GPCRPreprint

Zhang, X., Gao, K., Nie, J., Meng, H., Sun, X., Zhao, J., & Liu, X. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.25.645380 · Cited by 1

A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis

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G protein-coupled receptor diversity and evolution in the closest living relatives of MetazoaPreprint

Bayonas, A. G. D. L., & King, N. (2025) · eLife · doi:10.7554/elife.107467.3 · Cited by 1

Fine-Tuning of GPCR–Chemokine Interactions. Design and Identification of Chemokine Analogues as Receptor Agonists, Biased Agonists, and Antagonists

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Elucidation of the cell signaling pathways mediating innate immunity and host-pathogen interactions

Nabar, N. R. (2019) · Figshare

Structure of the antidiuretic hormone vasopressin receptor signalling complexPreprint

Bous, J., Orcel, H., Floquet, N., Leyrat, C., Lai‐Kee‐Him, J., Gaibelet, G., Ancelin, A., Saint‐Paul, J., Trapani, S., Louet, M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.22.424028

Das Konformationsgleichgewicht des Neuropeptid‐Y2‐Rezeptors in Lipidmembranen

Krug, U., Gloge, A., Schmidt, P. M., Becker‐Baldus, J., Bernhard, F., Kaiser, A., Montag, C., Gauglitz, M., Vishnivetskiy, S. A., Gurevich, V. V., et al. (2020) · Angewandte Chemie · doi:10.1002/ange.202006075

Design, Synthesis, and Evaluation of Novel, Multifunctional Dimethyltyrosine-Tetrahydroisoquinoline Opioid Peptidomimetics

Montgomery, D. (2019) · Deep Blue (University of Michigan)

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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