The Molecular Basis of G Protein–Coupled Receptor Activation

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

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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

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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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Probing biased activation of mu-opioid receptor by the biased agonist PZM21 using all atom molecular dynamics simulation

Liao, S., Tan, K., Floyd, C., Bong, D., Pino, M. J., & Wu, C. F. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119026 · Cited by 17

Insights into cellular signaling from membrane dynamics

Sarkar, P., & Chattopadhyay, A. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108794 · Cited by 17

Complementary biosensors reveal different G-protein signaling modes triggered by GPCRs and non-receptor activators

Garcia‐Marcos, M. (2021) · eLife · doi:10.7554/elife.65620 · Cited by 17

Addressing free fatty acid receptor 1 (FFAR1) activation using supervised molecular dynamics

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Gut-heart axis: cardiac remodeling and heart failure in the context of inflammatory bowel disease and dysbiosis

KOCHKARIAN, T., Nagy, H. I., & Li, Q. (2025) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00016.2025 · Cited by 18

The molecular basis of μ-opioid receptor signaling plasticity

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Molecular Dynamics Simulations of the Allosteric Modulation of the Adenosine A2a Receptor by a Mini-G Protein

Renault, P., Louet, M., Marie, J., Labesse, G., & Floquet, N. (2019) · Scientific Reports · doi:10.1038/s41598-019-41980-x · Cited by 16

Locating dynamic contributions to allostery via determining rates of vibrational energy transfer

Poudel, H., & Leitner, D. M. (2022) · The Journal of Chemical Physics · doi:10.1063/5.0132089 · Cited by 16

Expression Mapping and Functional Analysis of Orphan G-Protein-Coupled Receptor GPR158 in the Adult Mouse Brain Using a GPR158 Transgenic Mouse

Chang, J., Song, Z., Wei, S., Zhou, Y., Ju, J., Yao, P., Jiang, Y., Jin, H., Chi, X., & Li, N. (2023) · Biomolecules · doi:10.3390/biom13030479 · Cited by 16

Interplay between G protein-coupled receptors and nanotechnology

Jiang, Y., Li, Y., Fu, X., Wu, Y., Wang, R., Zhao, M., Mao, C., & Shi, S. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.07.049 · Cited by 16

Heterotrimeric G protein signaling without GPCRs: The Gα-binding-and-activating (GBA) motif

Garcia‐Marcos, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105756 · Cited by 16

Structural insights into KSHV-GPCR constitutive activation and CXCL1 chemokine recognition

Liu, A., Liu, Y., del Torrent, C. L., Zhang, W., Pardo, L., & Ye, R. D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403217121 · Cited by 17

Cholesterol-dependent endocytosis of GPCRs: implications in pathophysiology and therapeutics

Kumar, G. A., & Chattopadhyay, A. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00878-7 · Cited by 17

Dimerization of β2-adrenergic receptor is responsible for the constitutive activity subjected to inverse agonism

Kwon, Y., Kim, D., Jeong, M. G., Hong, M.-T., Park, S., Chang, Y., Zhou, K., Park, S., Zhang, J., & Ryu, S. H. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.09.001 · Cited by 16

The search for opioid analgesics with limited tolerance liability

Wtorek, K., Piekielna‐Ciesielska, J., Janecki, T., & Janecka, A. E. (2020) · Peptides · doi:10.1016/j.peptides.2020.170331 · Cited by 16

Adenosine: The common target between cancer immunotherapy and glaucoma in the eye

Hallaj, S., Mirza‐Aghazadeh‐Attari, M., Arasteh, A., Ghorbani, A., Lee, D., & Jadidi‐Niaragh, F. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119796 · Cited by 15

β2-adrenergic receptor regulates ER-mitochondria contacts

Lim, Y., Cho, I., Rennke, H. G., & Cho, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-00801-w · Cited by 18

G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling

Ge, H., Wang, H., Pan, B., Feng, D., Guo, C., Yang, L., Liu, D., & Wüthrich, K. (2022) · Molecules · doi:10.3390/molecules27092658 · Cited by 15

Elucidation of Partial Activation of Cannabinoid Receptor Type 2 and Identification of Potential Partial Agonist: Molecular Dynamics Simulation and Structure-Based Virtual Screening

Uba, A. İ., Aluwala, H., Liu, H., & Wu, C. F. (2022) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2022.107723 · Cited by 15

Mechanistic basis of GPCR activation explored by ensemble refinement of crystallographic structures

Madsen, J. J., Ye, L., Frimurer, T. M., & Olsen, O. H. (2022) · Protein Science · doi:10.1002/pro.4456 · Cited by 15

Integrative analysis of metabolomics and proteomics unravels purine metabolism dysregulation in the SOD1G93A mouse model of amyotrophic lateral sclerosis

Xu, X., Yang, Q., Liu, Z., Zhang, R., Yu, H., Wang, M., Chen, S., Xu, G., Shao, Y., & Le, W. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106110 · Cited by 17

NMR sample optimization and backbone assignment of a stabilized neurotensin receptor

Mohamadi, M., Goričanec, D., Wagner, G., & Hagn, F. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107970 · Cited by 15

GPCRs and fibroblast heterogeneity in fibroblast‐associated diseases

Dwivedi, N. V., Datta, S., El‐Kersh, K., Sadikot, R. T., Ganti, A. K., Batra, S. K., & Jain, M. (2023) · The FASEB Journal · doi:10.1096/fj.202301091 · Cited by 16

Illuminating the understudied GPCR-ome

Majumdar, S., Chiu, Y.-T., Pickett, J. E., & Roth, B. L. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103848 · Cited by 15

Direct Binding Methods to Measure Receptor–Ligand Interactions

Ray, M., Sayeed, A., Ganshert, M., & Saha, A. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c05041 · Cited by 15

Constitutive activation mechanism of a class C GPCR

Shin, J. W., Park, J., Jeong, J., Lam, J. H., Qiu, X., Wu, D., Kim, K., Lee, J., Robinson, C. V., Hyun, J., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01224-7 · Cited by 14

Established and emerging players in phospholipid scrambling: A structural perspective

Sebinelli, H. G., Syska, C., Čopič, A., & Lenoir, G. (2024) · Biochimie · doi:10.1016/j.biochi.2024.09.008 · Cited by 13

Molecular basis for chemokine recognition and activation of XCR1

Zhang, X., Schlimgen, R. R., Singh, S., Tomani, M., Volkman, B. F., & Zhang, C. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2405732121 · Cited by 15

Targeting serotonin receptors with phytochemicals – an in-silico study

Elalouf, A., Yaniv‐Rosenfeld, A., & Maoz, H. (2024) · Scientific Reports · doi:10.1038/s41598-024-76329-6 · Cited by 16

Cxcl10 Chemokine Induces Migration of ING4-Deficient Breast Cancer Cells via a Novel Cross Talk Mechanism between the Cxcr3 and Egfr Receptors

Tsutsumi, E., Stricklin, J., Peterson, E. A., Schroeder, J. A., & Kim, S. (2021) · Molecular and Cellular Biology · doi:10.1128/mcb.00382-21 · Cited by 15

Binding site identification of G protein-coupled receptors through a 3D Zernike polynomials-based method: application to C. elegans olfactory receptors

Rienzo, L. D., Flaviis, L. D., Ruocco, G., Folli, V., & Milanetti, E. (2022) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-021-00434-1 · Cited by 15

Exploring membrane organization at varying spatiotemporal resolutions utilizing fluorescence-based approaches: implications in membrane biology

Sarkar, P., & Chattopadhyay, A. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp02087j · Cited by 14

Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins

Ryazantsev, M. N., Nikolaev, D. M., Владимирович, С. А., & Brown, M. F. (2019) · The Journal of Membrane Biology · doi:10.1007/s00232-019-00095-0 · Cited by 17

Revealing the Positive Binding Cooperativity Mechanism between the Orthosteric and the Allosteric Antagonists of CCR2 by Metadynamics and Gaussian Accelerated Molecular Dynamics Simulations

An, X., Bai, Q., Bing, Z., Liu, H., Zhang, Q., Liu, H., & Yao, X. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00630 · Cited by 15

Role of Helix 8 in Dopamine Receptor Signaling

Yang, H.-S., Sun, N., Zhao, X., Kim, H. R., Park, H., Kim, K., & Chung, K. Y. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.026 · Cited by 14

The role of GPR110 in lung cancer progression

Ma, B., Zhu, J., Su, J., Pan, F., Ji, Y., Luan, L., Huang, J., & Hou, Y. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-3146 · Cited by 14

Two neuroendocrine G protein‐coupled receptor molecules, somatostatin and melatonin: Physiology of signal transduction and therapeutic perspectives

Costanzi, E., Simioni, C., Conti, I., Laface, I., Varano, G., Brenna, C., & Neri, L. M. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30062 · Cited by 14

β-Arrestin as a Therapeutic Target in Heart Failure

Boussi, L. S., & Frishman, W. H. (2020) · Cardiology in Review · doi:10.1097/crd.0000000000000363 · Cited by 14

Analysis of CCR2 splice variant expression patterns and functional properties

Park, H., Na, Y. H., Nguyen, H. T., Nguyen, L. P., Hurh, S., Seong, J. Y., Lee, C. S., Ham, B., & Hwang, J. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00787-6 · Cited by 14

The ADORA1 mutation linked to early-onset Parkinson’s disease alters adenosine A1-A2A receptor heteromer formation and function

Sarasola, L. I., del Torrent, C. L., Arévalo, A. P., Argerich, J., Casajuana-Martín, N., Chevigné, A., Fernández‐Dueñas, V., Ferré, S., Pardo, L., & Ciruela, F. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113896 · Cited by 14

The β2-adrenergic receptor agonist terbutaline upregulates T helper-17 cells in a protein kinase A-dependent manner

Gonczi, C. M. C., Hajiaghayi, M., Gholizadeh, F., Soares, M. A. X., Touma, F., Naranjo, C. L., Rios, A. J., Pozzebon, C., Daigneault, T., Burchell-Reyes, K., et al. (2023) · Human Immunology · doi:10.1016/j.humimm.2023.06.007 · Cited by 14

Design, Synthesis, and Application of Fluorescent Ligands Targeting the Intracellular Allosteric Binding Site of the CXC Chemokine Receptor 2

Casella, B. M., Farmer, J. P., Nesheva, D. N., Williams, H. E. L., Charlton, S. J., Holliday, N. D., Laughton, C. A., & Mistry, S. N. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00849 · Cited by 16

Structural diversity of leukotriene G-protein coupled receptors

Luginina, A. P., Gusach, A., Lyapina, E., Khorn, P. A., Safronova, N. A., Shevtsov, M. B., Dmitrieva, D. A., Dashevskii, D. E., Kotova, T., Smirnova, E., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105247 · Cited by 13

The fluorosis conundrum: bridging the gap between science and public health

Kumar, S., Chhabra, V., Mehra, M., Saranya, K., Kumar, H., Shenoy, S., Swamy, R. S., Murti, K., Pai, K. S. R., & Kumar, N. (2023) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2023.2268722 · Cited by 15

Cardiac human bitter taste receptors contain naturally occurring variants that alter function

Bloxham, C. J., Hulme, K. D., Fierro, F., Fercher, C., Pegg, C. L., O’Brien, S. L., Foster, S. R., Short, K. R., Furness, S. G. B., Reichelt, M. E., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115932 · Cited by 14

GLP-1/GIP Agonist as an Intriguing and Ultimate Remedy for Combating Alzheimer’s Disease through its Supporting DPP4 Inhibitors: A Review

Abubakar, M., Nama, L., Ansari, M. M., Ansari, M. M., Bhardwaj, S., Daksh, R., Syamala, K. L. V., Jamadade, M. S., Chhabra, V., Kumar, D., et al. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266293416240515075450 · Cited by 14

Molecular glues as potential GPCR therapeutics

Roth, B. L., & Krumm, B. E. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116402 · Cited by 14

Opioid receptors reveal a discrete cellular mechanism of endosomal G protein activation

Fisher, N. M., & von Zastrow, M. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2420623122 · Cited by 14

Peeking at G-protein-coupled Receptors Through the Molecular Dynamics Keyhole

Deganutti, G., Moro, S., & Reynolds, C. A. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0393 · Cited by 15

Modeling of CCR5 Recognition by HIV-1 gp120: How the Viral Protein Exploits the Conformational Plasticity of the Coreceptor

Jacquemard, C., Koensgen, F., Colin, P., Lagane, B., & Kellenberger, E. (2021) · Viruses · doi:10.3390/v13071395 · Cited by 14

Overcoming the Challenges of Detecting GPCR Oligomerization in the Brain

Fernández‐Dueñas, V., Bonaventura, J., Aso, E., Luján, R., Ferré, S., & Ciruela, F. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211104145727 · Cited by 14

A chromatographic method for pursuing potential GPCR ligands with the capacity to characterize their intrinsic activities of regulating downstream signaling pathway

Li, T., Zheng, X., Ou, Y., Ou, Y., Qiao, S., Zhao, X., Zhang, Y., Zhao, X., & Ma, Q. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.109792 · Cited by 14

A collage of cholesterol interaction motifs in the serotonin1A receptor: An evolutionary implication for differential cholesterol interaction.

Fatakia, S., Sarkar, P., & Chattopadhyay, A. (2019) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2019.02.010 · Cited by 13

Rescue of Cell Surface Expression and Signaling of Mutant Follicle-Stimulating Hormone Receptors

Hanyroup, S., Anderson, R. C., Nataraja, S. G., Yu, H. N., Millar, R. P., & Newton, C. L. (2021) · Endocrinology · doi:10.1210/endocr/bqab134 · Cited by 15

Physical biology of GPCR signalling dynamics inferred from fluorescence spectroscopy and imaging

Chavez-Abiega, S., Goedhart, J., & Bruggeman, F. J. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.05.007 · Cited by 13

Structural and dynamic insights into the biased signaling mechanism of the human kappa opioid receptor

Suno-Ikeda, C., Nishikawa, R., Suzuki, R., Yokoi, S., Iwata, S., Takai, T., Ogura, T., Hirose, M., Tokuda, A., Katamoto, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64882-1 · Cited by 13

Construction and Applications of Mammalian Cell-Based DNA-Encoded Peptide/Protein Libraries

Wang, Y., Zhang, K., Zhao, Y., Li, Y., Su, W., & Li, S. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00043 · Cited by 13

Protons taken hostage: Dynamic H-bond networks of the pH-sensing GPR68

Kapur, B. M., Baldessari, F., Lazaratos, M., Nar, H., Schnapp, G., Giorgetti, A., & Bondar, A. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.08.034 · Cited by 13

Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP

Luebbers, A., Gonzalez-Hernandez, A. J., Zhou, M., Eyles, S. J., Levitz, J., & Garcia-Marcos, M. (2024) · Structure · doi:10.1016/j.str.2023.10.010 · Cited by 13

Advances in ligand-specific biosensing for structurally similar molecules

Xi, C., Diao, J., & Moon, T. S. (2023) · Cell Systems · doi:10.1016/j.cels.2023.10.009 · Cited by 17

Artificial and Natural Sweeteners Biased T1R2/T1R3 Taste Receptors Transactivate Glycosylated Receptors on Cancer Cells to Induce Epithelial–Mesenchymal Transition of Metastatic Phenotype

Skapinker, E., Aldbai, R., Aucoin, E. B., Clarke, E., Clark, M., Ghokasian, D., Kombargi, H. L., Abraham, M. J., Li, Y., Bunsick, D. A., et al. (2024) · Nutrients · doi:10.3390/nu16121840 · Cited by 13

Chemokine CX3CL1 (Fractalkine) Signaling and Diabetic Encephalopathy

Wątroba, M., Grabowska, A. D., & Szukiewicz, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147527 · Cited by 13

Chemistry/structural biology of psychedelic drugs and their receptor(s)

Gumpper, R. H., & Nichols, D. E. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17361 · Cited by 14

5-HT6 receptors: Contemporary views on their neurobiological and pharmacological relevance in neuropsychiatric disorders

Chagraoui, A., Thibaut, F., & Deurwaerdère, P. D. (2025) · Dialogues in Clinical Neuroscience · doi:10.1080/19585969.2025.2502028 · Cited by 16

Enhanced Sampling and Tailored Collective Variables Yield Reproducible Free Energy Landscapes of Beta-1 Adrenergic Receptor Activation

Aureli, S., Rizzi, V., Piasentin, N., & Gervasio, F. L. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00600 · Cited by 13

Optogenetic Techniques for Manipulating and Sensing G Protein-Coupled Receptor Signaling

Abreu, N., & Levitz, J. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0755-8_2 · Cited by 16

Statistics for the analysis of molecular dynamics simulations: providing P values for agonist-dependent GPCR activation

Bruzzese, A., Dalton, J. A. R., & Giraldo, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-77072-4 · Cited by 13

SINAPs: A Software Tool for Analysis and Visualization of Interaction Networks of Molecular Dynamics Simulations

Bedart, C., Renault, N., Chavatte, P., Porcherie, A., Lachgar, A., Capron, M., & Farce, A. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00854 · Cited by 15

MD Simulations Revealing Special Activation Mechanism of Cannabinoid Receptor 1

Wu, Y., Li, X., Hua, T., Liu, Z., Liu, H., & Zhao, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.860035 · Cited by 13

Can Adding Constitutive Receptor Activity Redefine Biased Signaling Quantification?

Zhou, B., Hall, D. A., & Giraldo, J. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.01.002 · Cited by 13

Ligand Binding-Induced Structural Changes in the M2 Muscarinic Acetylcholine Receptor Revealed by Vibrational Spectroscopy

Katayama, K., Suzuki, K., Suno, R., Tsujimoto, H., Iwata, S., Kobayashi, T., & Kandori, H. (2019) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.9b02942 · Cited by 13

Structure of the agonist 12–HHT in its BLT2 receptor-bound state

Giusti, F., Casiraghi, M., Point, É., Damian, M., Rieger, J., Bon, C. L., Pozza, A., Moncoq, K., Banères, J., & Catoire, L. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-59571-6 · Cited by 13

Loss‐of‐function of Endothelin receptor type A results in Oro‐Oto‐Cardiac syndrome

Pritchard, A. B., Kanai, S. M., Krock, B. L., Schindewolf, E. M., Oliver-Krasinski, J. M., Khalek, N., Okashah, N., Lambert, N. A., Tavares, A. L. P., Zackai, E. H., et al. (2020) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61531 · Cited by 14

Understanding the Binding Specificity of G‑Protein Coupled Receptors toward G‑Proteins and Arrestins: Application to the Dopamine Receptor Family

Preto, A. J., Barreto, C. A. V., Baptista, S. J., de Almeida, J. G., Lemos, A., Melo, A., Cordeiro, M. N. D. S., Kurkcuoglu, Z., Melo, R., & Moreira, I. S. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00371 · Cited by 14

Pharmacology, Signaling and Therapeutic Potential of Metabotropic Glutamate Receptor 5 Negative Allosteric Modulators

Kos, J. A., Langiu, M., Hellyer, S. D., & Gregory, K. J. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00213 · Cited by 13

Convergent genome evolution shaped the emergence of terrestrial animals

Wei, J., Pisani, D., Donoghue, P. C. J., Álvarez‐Presas, M., & Paps, J. (2025) · Nature · doi:10.1038/s41586-025-09722-4 · Cited by 15

Ligand-specific activation trajectories dictate GPCR signalling in cells

Thomas, R., Jacoby, P. S., Faveri, C. D., Derieux, C., Liebing, A., Melkes, B., Martini, H.-J., Bermúdez, M., Stäubert, C., Lohse, M. J., et al. (2026) · Nature · doi:10.1038/s41586-025-09963-3 · Cited by 12

Vibrational spectroscopy analysis of ligand efficacy in human M2 muscarinic acetylcholine receptor (M2R)

Katayama, K., Suzuki, K., Suno, R., Kise, R., Tsujimoto, H., Iwata, S., Inoue, A., Kobayashi, T., & Kandori, H. (2021) · Communications Biology · doi:10.1038/s42003-021-02836-1 · Cited by 12

A Molecular Landscape of Mouse Hippocampal Neuromodulation

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Activation and Speciation Mechanisms in Class A GPCRs

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