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:

Noncanonical scaffolding of G αi and β-arrestin by G protein–coupled receptors
Jeffrey S. Smith, Thomas F. Pack, Asuka Inoue, et al.
Science (2021) Vol. 371, Iss. 6534
Open Access | Times Cited: 99

Showing 51-75 of 99 citing articles:

Generation of Comprehensive GPCR-Transducer-Deficient Cell Lines to Dissect the Complexity of GPCR Signaling
Ayaki Saito, Ryoji Kise, Asuka Inoue
Pharmacological Reviews (2024) Vol. 76, Iss. 4, pp. 599-619
Open Access | Times Cited: 2

Dynamic monitoring soft tissue healing via visualized Gd-crosslinked double network MRI microspheres
Tongtong Chen, Zhengwei Cai, Xinxin Zhao, et al.
Journal of Nanobiotechnology (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 2

IFN‐α/β‐mediated NK2R expression is related to the malignancy of colon cancer cells
Huihui Xiang, Yujiro Toyoshima, Weidong Shen, et al.
Cancer Science (2022) Vol. 113, Iss. 8, pp. 2513-2525
Open Access | Times Cited: 11

The ubiquitination status of the glucagon receptor determines signal bias
Suneet Kaur, Badr Sokrat, Megan E. Capozzi, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 5, pp. 104690-104690
Open Access | Times Cited: 6

T‐2 Toxin‐Mediated β‐Arrestin‐1 O‐GlcNAcylation Exacerbates Glomerular Podocyte Injury via Regulating Histone Acetylation
Tushuai Li, Wenxue Sun, Shenglong Zhu, et al.
Advanced Science (2023) Vol. 11, Iss. 7
Open Access | Times Cited: 6

Chemokine/GPCR Signaling-Mediated EMT in Cancer Metastasis
Xutengyue Tian, Jiayi Wang, Lanxin Jiang, et al.
Journal of Oncology (2022) Vol. 2022, pp. 1-15
Open Access | Times Cited: 9

Migration mediated by the oxysterol receptor GPR183 depends on arrestin coupling but not receptor internalization
Viktoria M. S. Kjær, Viktorija Daugvilaite, Tomasz Maciej Stępniewski, et al.
Science Signaling (2023) Vol. 16, Iss. 779
Closed Access | Times Cited: 5

A2B adenosine receptor activation and modulation by protein kinase C
Zhan‐Guo Gao, Ian M. Levitan, Asuka Inoue, et al.
iScience (2023) Vol. 26, Iss. 7, pp. 107178-107178
Open Access | Times Cited: 5

Noncanonical interactions of G proteins and β‐arrestins: from competitors to companions
Jeffrey S. Smith, Thomas F. Pack
FEBS Journal (2021) Vol. 288, Iss. 8, pp. 2550-2561
Open Access | Times Cited: 12

Ciliary Type III Adenylyl Cyclase in the VMH Is Crucial for High‐Fat Diet‐Induced Obesity Mediated by Autophagy
Dong Yang, Xiangbo Wu, Weina Wang, et al.
Advanced Science (2021) Vol. 9, Iss. 3
Open Access | Times Cited: 11

A GPCR screening in human keratinocytes identifies that the metabolite receptor HCAR3 controls epithelial proliferation, migration, and cellular respiration
M. Pilar Pedro, Katherine Lund, Sun Woo Sophie Kang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4

β-Arrestin-dependent and -independent endosomal G protein activation by the vasopressin type 2 receptor
Carole Daly, Akim Abdul Guseinov, Hyunggu Hahn, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 4

Association of Neurokinin-1 Receptor Signaling Pathways with Cancer
Francisco D. Rodríguez, Rafael Coveñas
Current Medicinal Chemistry (2023) Vol. 31, Iss. 39, pp. 6460-6486
Closed Access | Times Cited: 4

β-Arrestin-dependent and -independent endosomal G protein activation by the vasopressin type 2 receptor
Carole Daly, Akim Abdul Guseinov, Hyunggu Hahn, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 4

Fluorescent biosensors illuminate the spatial regulation of cell signaling across scales
Anne C. Lyons, Sohum Mehta, Jin Zhang
Biochemical Journal (2023) Vol. 480, Iss. 20, pp. 1693-1717
Open Access | Times Cited: 4

ACKR3 Proximity Labeling Identifies Novel G protein- and β-arrestin-independent GPCR Interacting Proteins
Chloe Hicks, Julia Gardner, Dylan Scott Eiger, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Single-molecule detection of transient dimerization of opioid receptors 1: Homodimers' effect on signaling and internalization
Peng Zhou, Taka A. Tsunoyama, Rinshi S. Kasai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Structural Rearrangement of the AT1 Receptor Modulated by Membrane Thickness and Tension
Bharat Poudel, Juan M. Vanegas
The Journal of Physical Chemistry B (2024)
Closed Access | Times Cited: 1

VPS26 Moonlights as a β-Arrestin-like Adapter for a 7-Transmembrane RGS Protein in Arabidopsis thaliana
Fei Lou, Wenbin Zhou, Meral Tunc‐Ozdemir, et al.
Biochemistry (2024) Vol. 63, Iss. 22, pp. 2990-2999
Open Access | Times Cited: 1

Serodolin, a β-arrestin–biased ligand of 5-HT 7 receptor, attenuates pain-related behaviors
Chayma El Khamlichi, Flora Reverchon, Nadège Hervouet‐Coste, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 21
Open Access | Times Cited: 7

Michaelis-Menten quantification of ligand signalling bias applied to the promiscuous Vasopressin V2 receptor
Franziska M. Heydenreich, Bianca Plouffe, Aurélien Rizk, et al.
Molecular Pharmacology (2022), pp. MOLPHARM-000497
Open Access | Times Cited: 7

Endosomal Chemokine Receptor Signalosomes Regulate Central Mechanisms Underlying Cell Migration
Hyunggu Hahn, Carole Daly, John R. Little, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

Gαs is dispensable for β-arrestin coupling but dictates GRK selectivity and is predominant for gene expression regulation by β2-adrenergic receptor
Valeria Burghi, Justine S. Paradis, Adam Officer, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 11, pp. 105293-105293
Open Access | Times Cited: 3

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