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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 control of δ-opioid receptor signalling
Gustavo Fenalti, Patrick M. Giguère, Vsevolod Katritch, et al.
Nature (2014) Vol. 506, Iss. 7487, pp. 191-196
Open Access | Times Cited: 475

Showing 26-50 of 475 citing articles:

GPCR activation mechanisms across classes and macro/microscales
Alexander S. Hauser, Albert J. Kooistra, Christian Munk, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 11, pp. 879-888
Open Access | Times Cited: 187
Biased Allosteric Modulators: New Frontiers in GPCR Drug Discovery
Lauren M. Slosky, Marc G. Caron, Lawrence S Barak
Trends in Pharmacological Sciences (2021) Vol. 42, Iss. 4, pp. 283-299
Open Access | Times Cited: 136
Interpretable bilinear attention network with domain adaptation improves drug–target prediction
Peizhen Bai, Filip Miljković, Bino John, et al.
Nature Machine Intelligence (2023) Vol. 5, Iss. 2, pp. 126-136
Closed Access | Times Cited: 125
International Union of Basic and Clinical Pharmacology. CXII: Adenosine Receptors: A Further Update
Adriaan P. IJzerman, Kenneth A. Jacobson, Christa E. Müller, et al.
Pharmacological Reviews (2022) Vol. 74, Iss. 2, pp. 340-372
Open Access | Times Cited: 105
Structures of the entire human opioid receptor family
Yue Wang, Youwen Zhuang, Jeffrey F. DiBerto, et al.
Cell (2023) Vol. 186, Iss. 2, pp. 413-427.e17
Open Access | Times Cited: 103
Structure determination of inactive-state GPCRs with a universal nanobody
Michael J. Robertson, Makaía M. Papasergi-Scott, Feng He, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 12, pp. 1188-1195
Open Access | Times Cited: 82
Structure-based design of bitopic ligands for the µ-opioid receptor
Abdelfattah Faouzi, Haoqing Wang, Saheem A. Zaidi, et al.
Nature (2022) Vol. 613, Iss. 7945, pp. 767-774
Closed Access | Times Cited: 82
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: 2
Metal Ion Signaling in Biomedicine
Raphaël Rodriguez, Sebastian Müller, Ludovic Colombeau, et al.
Chemical Reviews (2025)
Open Access | Times Cited: 2
Biased and G Protein-Independent Signaling of Chemokine Receptors
Anne Steen, Olav Larsen, Stefanie Thiele, et al.
Frontiers in Immunology (2014) Vol. 5
Open Access | Times Cited: 168
Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor
Haitao Zhang, Hamiyet Ünal, Russell Desnoyer, et al.
Journal of Biological Chemistry (2015) Vol. 290, Iss. 49, pp. 29127-29139
Open Access | Times Cited: 167
Structural basis for bifunctional peptide recognition at human δ-opioid receptor
Gustavo Fenalti, Nadia A. Zatsepin, Cecilia Betti, et al.
Nature Structural & Molecular Biology (2015) Vol. 22, Iss. 3, pp. 265-268
Open Access | Times Cited: 165
Structure of CC Chemokine Receptor 5 with a Potent Chemokine Antagonist Reveals Mechanisms of Chemokine Recognition and Molecular Mimicry by HIV
Yi Zheng, Gye Won Han, Ruben Abagyan, et al.
Immunity (2017) Vol. 46, Iss. 6, pp. 1005-1017.e5
Open Access | Times Cited: 161
Structural Connection between Activation Microswitch and Allosteric Sodium Site in GPCR Signaling
Kate L. White, Matthew T. Eddy, Zhan‐Guo Gao, et al.
Structure (2018) Vol. 26, Iss. 2, pp. 259-269.e5
Open Access | Times Cited: 159
Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations
Libin Ye, Chris Neale, Adnan Sljoka, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 147
Diverse GPCRs exhibit conserved water networks for stabilization and activation
AJ Venkatakrishnan, Karen Anthony, Rasmus Fonseca, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 8, pp. 3288-3293
Open Access | Times Cited: 144
Endogenous Allosteric Modulators of G Protein–Coupled Receptors
Emma T. van der Westhuizen, Céline Valant, Patrick M. Sexton, et al.
Journal of Pharmacology and Experimental Therapeutics (2015) Vol. 353, Iss. 2, pp. 246-260
Open Access | Times Cited: 137
Allosteric Modulation of Class A GPCRs: Targets, Agents, and Emerging Concepts
Eric A. Wold, Jianping Chen, Kathryn A. Cunningham, et al.
Journal of Medicinal Chemistry (2018) Vol. 62, Iss. 1, pp. 88-127
Open Access | Times Cited: 132
Structural Basis for G Protein–Coupled Receptor Signaling
Sarah C. Erlandson, Conor McMahon, Andrew C. Kruse
Annual Review of Biophysics (2018) Vol. 47, Iss. 1, pp. 1-18
Open Access | Times Cited: 131
Identification of a Conformational Equilibrium That Determines the Efficacy and Functional Selectivity of the μ‐Opioid Receptor
Junya Okude, Takumi Ueda, Yutaka Kofuku, et al.
Angewandte Chemie International Edition (2015) Vol. 54, Iss. 52, pp. 15771-15776
Open Access | Times Cited: 125
Orthosteric and allosteric action of the C5a receptor antagonists
Heng Liu, Hee Ryung Kim, R. N. V. Krishna Deepak, et al.
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 6, pp. 472-481
Closed Access | Times Cited: 123
New Binding Sites, New Opportunities for GPCR Drug Discovery
H. C. Stephen Chan, Yi Li, Thamani Dahoun, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 4, pp. 312-330
Open Access | Times Cited: 123
What Can Crystal Structures of Aminergic Receptors Tell Us about Designing Subtype-Selective Ligands?
Mayako Michino, Thijs Beuming, Prashant Donthamsetti, et al.
Pharmacological Reviews (2014) Vol. 67, Iss. 1, pp. 198-213
Open Access | Times Cited: 118
A biomimetic approach for enhancing the in vivo half-life of peptides
Sravan Penchala, Mark R. Miller, Arindom Pal, et al.
Nature Chemical Biology (2015) Vol. 11, Iss. 10, pp. 793-798
Open Access | Times Cited: 118
Structural Basis for Apelin Control of the Human Apelin Receptor
Yingli Ma, Yang Yue, Yanbin Ma, et al.
Structure (2017) Vol. 25, Iss. 6, pp. 858-866.e4
Open Access | Times Cited: 118

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