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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor
Yang Lee, Tony Warne, Rony Nehmé, et al.
Nature (2020) Vol. 583, Iss. 7818, pp. 862-866
Open Access | Times Cited: 234

Showing 1-25 of 234 citing articles:

G protein-coupled receptors: structure- and function-based drug discovery
Dehua Yang, Qingtong Zhou, Viktorija Labroska, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 433
Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor
Kuglae Kim, Tao Che, Ouliana Panova, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1574-1588.e19
Open Access | Times Cited: 375
Conformational Basis of G Protein-Coupled Receptor Signaling Versatility
Laura M. Wingler, Robert J. Lefkowitz
Trends in Cell Biology (2020) Vol. 30, Iss. 9, pp. 736-747
Open Access | Times Cited: 192
Molecular recognition of morphine and fentanyl by the human μ-opioid receptor
Youwen Zhuang, Yue Wang, Bingqing He, et al.
Cell (2022) Vol. 185, Iss. 23, pp. 4361-4375.e19
Open Access | Times Cited: 155
Structure-Based Virtual Screening for Ligands of G Protein–Coupled Receptors: What Can Molecular Docking Do for You?
Flavio Ballante, Albert J. Kooistra, Stefanie Kampen, et al.
Pharmacological Reviews (2021) Vol. 73, Iss. 4, pp. 1698-1736
Open Access | Times Cited: 104
Signaling snapshots of a serotonin receptor activated by the prototypical psychedelic LSD
Can Cao, Ximena Barros-Álvarez, Shicheng Zhang, et al.
Neuron (2022) Vol. 110, Iss. 19, pp. 3154-3167.e7
Open Access | Times Cited: 102
Serial femtosecond crystallography
Thomas R. M. Barends, Benjamin Stauch, Vadim Cherezov, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 86
Heterotrimeric Gq proteins act as a switch for GRK5/6 selectivity underlying β-arrestin transducer bias
Kouki Kawakami, Masataka Yanagawa, Suzune Hiratsuka, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 77
GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision
Wesley B. Asher, Daniel S. Terry, G. Glenn Gregorio, et al.
Cell (2022) Vol. 185, Iss. 10, pp. 1661-1675.e16
Open Access | Times Cited: 76
Structure of the vasopressin hormone–V2 receptor–β-arrestin1 ternary complex
Julien Bous, Aurélien Fouillen, Hélène Orcel, et al.
Science Advances (2022) Vol. 8, Iss. 35
Open Access | Times Cited: 75
GPCR activation and GRK2 assembly by a biased intracellular agonist
Jia Duan, Heng Liu, Fenghui Zhao, et al.
Nature (2023) Vol. 620, Iss. 7974, pp. 676-681
Open Access | Times Cited: 56
β−Arrestins: Structure, Function, Physiology, and Pharmacological Perspectives
Jürgen Wess, Antwi‐Boasiako Oteng, Osvaldo Rivera‐Gonzalez, et al.
Pharmacological Reviews (2023) Vol. 75, Iss. 5, pp. 854-884
Open Access | Times Cited: 55
Nanobodies: Robust miniprotein binders in biomedicine
Jeffrey Yong Joon Kim, Zhe Sang, Yufei Xiang, et al.
Advanced Drug Delivery Reviews (2023) Vol. 195, pp. 114726-114726
Open Access | Times Cited: 43
Plasma membrane preassociation drives β-arrestin coupling to receptors and activation
Jak Grimes, Zsombor Kőszegi, Yann Lanoiselée, et al.
Cell (2023) Vol. 186, Iss. 10, pp. 2238-2255.e20
Open Access | Times Cited: 42
Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation
Jagannath Maharana, Parishmita Sarma, Manish K. Yadav, et al.
Molecular Cell (2023) Vol. 83, Iss. 12, pp. 2091-2107.e7
Open Access | Times Cited: 42
Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors
Jagannath Maharana, Fumiya K. Sano, Parishmita Sarma, et al.
Science (2024) Vol. 383, Iss. 6678, pp. 101-108
Open Access | Times Cited: 17
Beneath the surface: endosomal GPCR signaling
Emmanuel Flores-Espinoza, A. Thomsen
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 6, pp. 520-531
Closed Access | Times Cited: 17
Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery
Paolo Conflitti, Edward Lyman, Mark S.P. Sansom, et al.
Nature Reviews Drug Discovery (2025)
Closed Access | Times Cited: 3
Nanodiscs: A toolkit for membrane protein science
Stephen G. Sligar, Ilia G. Denisov
Protein Science (2020) Vol. 30, Iss. 2, pp. 297-315
Open Access | Times Cited: 114
Intrinsic bias at non-canonical, β-arrestin-coupled seven transmembrane receptors
Shubhi Pandey, Punita Kumari, Mithu Baidya, et al.
Molecular Cell (2021) Vol. 81, Iss. 22, pp. 4605-4621.e11
Open Access | Times Cited: 86
Structure determination of GPCRs: cryo-EM compared with X-ray crystallography
Javier García‐Nafría, Christopher G. Tate
Biochemical Society Transactions (2021) Vol. 49, Iss. 5, pp. 2345-2355
Open Access | Times Cited: 85
G protein-coupled receptor-G protein interactions: a single-molecule perspective
Davide Calebiro, Zsombor Kőszegi, Yann Lanoiselée, et al.
Physiological Reviews (2020) Vol. 101, Iss. 3, pp. 857-906
Open Access | Times Cited: 82
The role of structural dynamics in GPCR‐mediated signaling
Daniel Hilger
FEBS Journal (2021) Vol. 288, Iss. 8, pp. 2461-2489
Open Access | Times Cited: 80
Arrestin-Dependent and -Independent Internalization of G Protein–Coupled Receptors: Methods, Mechanisms, and Implications on Cell Signaling
Ee Von Moo, Jeffrey R. van Senten, Hans Bräuner‐Osborne, et al.
Molecular Pharmacology (2021) Vol. 99, Iss. 4, pp. 242-255
Open Access | Times Cited: 75
Ligands of Adrenergic Receptors: A Structural Point of View
Yiran Wu, Liting Zeng, Suwen Zhao
Biomolecules (2021) Vol. 11, Iss. 7, pp. 936-936
Open Access | Times Cited: 69
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