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:

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

Showing 1-25 of 42 citing articles:

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

Molecular insights into intrinsic transducer-coupling bias in the CXCR4-CXCR7 system
Parishmita Sarma, Carlo Marion C. Carino, Deeksha Seetharama, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 27

Cryo-electron microscopy for GPCR research and drug discovery in endocrinology and metabolism
Jia Duan, Xinheng He, Shujie Li, et al.
Nature Reviews Endocrinology (2024) Vol. 20, Iss. 6, pp. 349-365
Closed Access | Times Cited: 13

ACKR3–arrestin2/3 complexes reveal molecular consequences of GRK-dependent barcoding
Qiuyan Chen, Christopher T. Schafer, Somnath Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 21

Location bias: A “Hidden Variable” in GPCR pharmacology
Dylan Scott Eiger, Chloe Hicks, Julia Gardner, et al.
BioEssays (2023) Vol. 45, Iss. 11
Closed Access | Times Cited: 14

Arrestin‐centred interactions at the membrane and their conformational determinants
Owen Underwood, Raphael S. Haider, Julie Sanchez, et al.
British Journal of Pharmacology (2024)
Open Access | Times Cited: 5

LIPIDS MODULATE THE DYNAMICS OF GPCR:β-ARRESTIN INTERACTION
Antoniel Augusto Severo Gomes, Michela Di Michele, Rita Roessner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4

Transient, nano-scale, liquid-like molecular assemblies coming of age
Akihiro Kusumi, Taka A. Tsunoyama, Kenichi Suzuki, et al.
Current Opinion in Cell Biology (2024) Vol. 89, pp. 102394-102394
Open Access | Times Cited: 4

Functional consequences of spatial, temporal and ligand bias of G protein-coupled receptors
András Dávid Tóth, Gábor Turu, László Hunyady
Nature Reviews Nephrology (2024) Vol. 20, Iss. 11, pp. 722-741
Closed Access | Times Cited: 4

Structural Diversity of Metabotropic Glutamate Receptor/Beta-Arrestin Coupling
Dagan C. Marx, Alberto J. Gonzalez-Hernandez, Kevin W. Huynh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access

MRGPRX2 ligandome: Molecular simulations reveal three categories of ligand-receptor interactions
Philip Maier, Moritz Macht, Silvan Beck, et al.
Journal of Structural Biology (2025), pp. 108193-108193
Closed Access

Distinct Membrane Binding Properties of the Two Non-visual Arrestins
Thomas D. Killeen, Katelyn R. Tepper, Kyle W. Miller, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access

cFos-mediated β-Arrestin1 in the RVLM alleviates sympathetic hyperactivity induced by ovariectomy
Jiuqiong Yan, Meng Qi, Hao Fan, et al.
Molecular and Cellular Endocrinology (2025), pp. 112520-112520
Closed Access

β-Arrestin Condensates Regulate G Protein-Coupled Receptor Function
Preston J. Anderson, Peng Xiao, Ya-Ni Zhong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

Isoprenaline shows unique kinase dependencies in stimulating β1AR–β-arrestin2 interaction compared to endogenous catecholamines
Edda S. F. Matthees, Luca E. Kletzin, Arnelle Löbbert, et al.
Molecular Pharmacology (2025), pp. 100041-100041
Closed Access

Exploring GPCR conformational dynamics using single-molecule fluorescence
Eugene Agyemang, Alyssa Gonneville, Sriram Tiruvadi Krishnan, et al.
Methods (2024) Vol. 226, pp. 35-48
Closed Access | Times Cited: 3

Role of the V2R–βarrestin–Gβγ complex in promoting G protein translocation to endosomes
Badr Sokrat, Anthony H. Nguyen, A. Thomsen, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 3

Neurokinin 1 Receptor Endocytosis and Signaling
Francisco D. Rodríguez, Rafael Coveñas
˜The œReceptors (2025), pp. 325-346
Closed Access

β1-Adrenergic Receptor Endocytosis and Signaling
Abdul Rouf War, M. K. Borah, Sarfraz Ahmed, et al.
˜The œReceptors (2025), pp. 99-118
Closed Access

Distinct activation mechanisms of β-arrestin-1 revealed by 19F NMR spectroscopy
Ruibo Zhai, Zhuoqi Wang, Zhaofei Chai, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 8

From membrane to nucleus: A three-wave hypothesis of cAMP signaling
Alejandro Pizzoni, Xuefeng Zhang, Daniel L. Altschuler
Journal of Biological Chemistry (2023) Vol. 300, Iss. 1, pp. 105497-105497
Open Access | Times Cited: 7

Information Transmission in G Protein-Coupled Receptors
Roger D. Jones
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 3, pp. 1621-1621
Open Access | Times Cited: 2

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