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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:

Activation of G-protein-coupled receptors correlates with the formation of a continuous internal water pathway
Shuguang Yuan, Sławomir Filipek, Krzysztof Palczewski, et al.
Nature Communications (2014) Vol. 5, Iss. 1
Open Access | Times Cited: 223

Showing 1-25 of 223 citing articles:

GPCR Dynamics: Structures in Motion
Naomi R. Latorraca, AJ Venkatakrishnan, Ron O. Dror
Chemical Reviews (2016) Vol. 117, Iss. 1, pp. 139-155
Open Access | Times Cited: 674
Common activation mechanism of class A GPCRs
Qingtong Zhou, Dehua Yang, Meng Wu, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 522
Structure and function of serotonin G protein-coupled receptors
John D. McCorvy, Bryan L. Roth
Pharmacology & Therapeutics (2015) Vol. 150, pp. 129-142
Open Access | Times Cited: 308
Structural insights into G-protein-coupled receptor allostery
David M. Thal, Alisa Glukhova, Patrick M. Sexton, et al.
Nature (2018) Vol. 559, Iss. 7712, pp. 45-53
Closed Access | Times Cited: 303
Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region
AJ Venkatakrishnan, Xavier Deupí, Guillaume Lebon, et al.
Nature (2016) Vol. 536, Iss. 7617, pp. 484-487
Open Access | Times Cited: 293
Activation and Signaling Mechanism Revealed by Cannabinoid Receptor-Gi Complex Structures
Tian Hua, Xiaoting Li, Lijie Wu, et al.
Cell (2020) Vol. 180, Iss. 4, pp. 655-665.e18
Open Access | Times Cited: 289
Molecular mechanism of biased signaling in a prototypical G protein–coupled receptor
Carl‐Mikael Suomivuori, Naomi R. Latorraca, Laura M. Wingler, et al.
Science (2020) Vol. 367, Iss. 6480, pp. 881-887
Open Access | Times Cited: 211
Structural basis of CXC chemokine receptor 2 activation and signalling
Kaiwen Liu, Lijie Wu, Shuguang Yuan, et al.
Nature (2020) Vol. 585, Iss. 7823, pp. 135-140
Closed Access | Times Cited: 195
GPCRmd uncovers the dynamics of the 3D-GPCRome
Ismael Rodríguez‐Espigares, Mariona Torrens‐Fontanals, Johanna K. S. Tiemann, et al.
Nature Methods (2020) Vol. 17, Iss. 8, pp. 777-787
Open Access | Times Cited: 141
GWAS of random glucose in 476,326 individuals provide insights into diabetes pathophysiology, complications and treatment stratification
Vasiliki Lagou, Longda Jiang, Anna Ulrich, et al.
Nature Genetics (2023) Vol. 55, Iss. 9, pp. 1448-1461
Open Access | Times Cited: 45
Systematic analysis of biomolecular conformational ensembles with PENSA
Martin Vögele, Neil J. Thomson, Sang Truong, et al.
The Journal of Chemical Physics (2025) Vol. 162, Iss. 1
Closed Access | Times Cited: 2
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
The Roles of Water in the Protein Matrix: A Largely Untapped Resource for Drug Discovery
Francesca Spyrakis, Mostafa H. Ahmed, Alexander S. Bayden, et al.
Journal of Medicinal Chemistry (2017) Vol. 60, Iss. 16, pp. 6781-6827
Open Access | Times Cited: 137
Molecular switches in GPCRs
Sławomir Filipek
Current Opinion in Structural Biology (2019) Vol. 55, pp. 114-120
Closed Access | Times Cited: 109
Harnessing Ion-Binding Sites for GPCR Pharmacology
Barbara Zarzycka, Saheem A. Zaidi, Bryan L. Roth, et al.
Pharmacological Reviews (2019) Vol. 71, Iss. 4, pp. 571-595
Open Access | Times Cited: 109
Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations
Samuel Hertig, Naomi R. Latorraca, Ron O. Dror
PLoS Computational Biology (2016) Vol. 12, Iss. 6, pp. e1004746-e1004746
Open Access | Times Cited: 105
The Fragment Molecular Orbital Method Reveals New Insight into the Chemical Nature of GPCR–Ligand Interactions
Alexander Heifetz, Ewa I. Chudyk, Laura Gleave, et al.
Journal of Chemical Information and Modeling (2015) Vol. 56, Iss. 1, pp. 159-172
Open Access | Times Cited: 103
Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines
D. Thirumalai, Changbong Hyeon, Pavel I. Zhuravlev, et al.
Chemical Reviews (2019) Vol. 119, Iss. 12, pp. 6788-6821
Open Access | Times Cited: 101
Structural basis of ligand interaction with atypical chemokine receptor 3
Martin Gustavsson, Liwen Wang, Noortje van Gils, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 95
Cholesterol-dependent Conformational Plasticity in GPCR Dimers
Xavier Prasanna, Durba Sengupta, Amitabha Chattopadhyay
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 89
Intracellular Transfer of Na+ in an Active-State G-Protein-Coupled Receptor
Owen N. Vickery, Catarina A. Carvalheda, Saheem A. Zaidi, et al.
Structure (2017) Vol. 26, Iss. 1, pp. 171-180.e2
Open Access | Times Cited: 89
Bitter taste receptors: Novel insights into the biochemistry and pharmacology
Appalaraju Jaggupilli, Ryan Howard, Jasbir Upadhyaya, et al.
The International Journal of Biochemistry & Cell Biology (2016) Vol. 77, pp. 184-196
Closed Access | Times Cited: 88
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: 78
Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
Jan Niclas Frei, R. William Broadhurst, Mark J. Bostock, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 75
Structural insights into emergent signaling modes of G protein–coupled receptors
Ieva Sutkevičiu̅tė, Jean‐Pierre Vilardaga
Journal of Biological Chemistry (2020) Vol. 295, Iss. 33, pp. 11626-11642
Open Access | Times Cited: 73
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