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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:

X-ray structures define human P2X3 receptor gating cycle and antagonist action
Steven Mansoor, Wei Lü, Wout Oosterheert, et al.
Nature (2016) Vol. 538, Iss. 7623, pp. 66-71
Open Access | Times Cited: 236

Showing 1-25 of 236 citing articles:

The P2X7 Receptor in Infection and Inflammation
Francesco Di Virgilio, Diego Dal Ben, Alba Clara Sarti, et al.
Immunity (2017) Vol. 47, Iss. 1, pp. 15-31
Open Access | Times Cited: 993
Structure of the mechanically activated ion channel Piezo1
Kei Saotome, Swetha E. Murthy, Jennifer M. Kefauver, et al.
Nature (2017) Vol. 554, Iss. 7693, pp. 481-486
Open Access | Times Cited: 507
Emerging Diversity in Lipid–Protein Interactions
Valentina Corradi, Besian I. Sejdiu, Haydeé Mesa‐Galloso, et al.
Chemical Reviews (2019) Vol. 119, Iss. 9, pp. 5775-5848
Open Access | Times Cited: 421
The P2X7 receptor: A main player in inflammation
Elena Adinolfi, Anna Lisa Giuliani, Elena De Marchi, et al.
Biochemical Pharmacology (2017) Vol. 151, pp. 234-244
Open Access | Times Cited: 326
Structural basis for subtype-specific inhibition of the P2X7 receptor
Akira Karasawa, Toshimitsu Kawate
eLife (2016) Vol. 5
Open Access | Times Cited: 263
Update of P2X receptor properties and their pharmacology: IUPHAR Review 30
Péter Illés, Christa E. Müller, Kenneth A. Jacobson, et al.
British Journal of Pharmacology (2020) Vol. 178, Iss. 3, pp. 489-514
Open Access | Times Cited: 244
Characterization of Lipid–Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation
Mélanie Müller, Tao Jiang, Chang Sun, et al.
Chemical Reviews (2019) Vol. 119, Iss. 9, pp. 6086-6161
Open Access | Times Cited: 240
The Elusive P2X7 Macropore
Francesco Di Virgilio, Günther Schmalzing, F Markwárdt
Trends in Cell Biology (2018) Vol. 28, Iss. 5, pp. 392-404
Closed Access | Times Cited: 230
Full-Length P2X7 Structures Reveal How Palmitoylation Prevents Channel Desensitization
Alanna E. McCarthy, Craig Yoshioka, Steven Mansoor
Cell (2019) Vol. 179, Iss. 3, pp. 659-670.e13
Open Access | Times Cited: 208
The P2X7 Receptor
Ronald Sluyter
Advances in experimental medicine and biology (2017), pp. 17-53
Closed Access | Times Cited: 191
P2X7 Interactions and Signaling – Making Head or Tail of It
R. Kopp, Anna Krautloher, Antonio Ramírez-Fernández, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 186
P2X receptor channels in chronic pain pathways
Louis‐Philippe Bernier, Ariel R. Ase, Philippe Séguéla
British Journal of Pharmacology (2017) Vol. 175, Iss. 12, pp. 2219-2230
Open Access | Times Cited: 172
P2X7 receptor and the NLRP3 inflammasome: Partners in crime
Pablo Pelegrı́n
Biochemical Pharmacology (2020) Vol. 187, pp. 114385-114385
Closed Access | Times Cited: 148
Neuronal P2X7 Receptors Revisited: Do They Really Exist?
Péter Illés, Tahir Muhammad Khan, Patrizia Rubini
Journal of Neuroscience (2017) Vol. 37, Iss. 30, pp. 7049-7062
Open Access | Times Cited: 157
The P2X7 Receptor-Interleukin-1 Liaison
Anna Lisa Giuliani, Alba Clara Sarti, Simonetta Falzoni, et al.
Frontiers in Pharmacology (2017) Vol. 8
Open Access | Times Cited: 156
The P2X7 receptor forms a dye-permeable pore independent of its intracellular domain but dependent on membrane lipid composition
Akira Karasawa, Kevin Michalski, Polina Mikhelzon, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 136
P2X7 in Cancer: From Molecular Mechanisms to Therapeutics
Romain Lara, Elena Adinolfi, Catherine Α. Harwood, et al.
Frontiers in Pharmacology (2020) Vol. 11
Open Access | Times Cited: 136
PyContact: Rapid, Customizable, and Visual Analysis of Noncovalent Interactions in MD Simulations
Maximilian Scheurer, P. J. Rodenkirch, Marc Siggel, et al.
Biophysical Journal (2018) Vol. 114, Iss. 3, pp. 577-583
Open Access | Times Cited: 127
The dual‐gate model for pentameric ligand‐gated ion channels activation and desensitization
Marc Gielen, Pierre‐Jean Corringer
The Journal of Physiology (2018) Vol. 596, Iss. 10, pp. 1873-1902
Open Access | Times Cited: 111
Lipids and ions traverse the membrane by the same physical pathway in the nhTMEM16 scramblase
Tao Jiang, Kuai Yu, H. Criss Hartzell, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 101
Druggable negative allosteric site of P2X3 receptors
Jin Wang, Yao Wang, Wen-Wen Cui, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 19, pp. 4939-4944
Open Access | Times Cited: 99
Ligand recognition and gating mechanism through three ligand-binding sites of human TRPM2 channel
Yihe Huang, Rebecca Roth, Wei Lü, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 97
On the permeation of large organic cations through the pore of ATP-gated P2X receptors
Mahboubi Harkat, Laurie Peverini, Adrien Henri Cerdan, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 19
Open Access | Times Cited: 94
Structural basis for pharmacological modulation of the TRPC6 channel
Yonghong Bai, Xinchao Yu, Hao Chen, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 94
Structural insights into the competitive inhibition of the ATP-gated P2X receptor channel
Go Kasuya, Toshiaki Yamaura, Xiaobo Ma, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 90
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