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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:

D 4 dopamine receptor high-resolution structures enable the discovery of selective agonists
Sheng Wang, Daniel Wacker, Anat Levit, et al.
Science (2017) Vol. 358, Iss. 6361, pp. 381-386
Open Access | Times Cited: 213

Showing 1-25 of 213 citing articles:

Ultra-large library docking for discovering new chemotypes
Jiankun Lyu, Sheng Wang, Trent E. Balius, et al.
Nature (2019) Vol. 566, Iss. 7743, pp. 224-229
Open Access | Times Cited: 772
Structure of the D2 dopamine receptor bound to the atypical antipsychotic drug risperidone
Sheng Wang, Tao Che, Anat Levit, et al.
Nature (2018) Vol. 555, Iss. 7695, pp. 269-273
Open Access | Times Cited: 390
Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor
Kuglae Kim, Tao Che, Ouliana Panova, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1574-1588.e19
Open Access | Times Cited: 374
A practical guide to large-scale docking
Brian J. Bender, Stefan Gahbauer, Andreas Luttens, et al.
Nature Protocols (2021) Vol. 16, Iss. 10, pp. 4799-4832
Open Access | Times Cited: 373
Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor
Tao Che, Susruta Majumdar, Saheem A. Zaidi, et al.
Cell (2018) Vol. 172, Iss. 1-2, pp. 55-67.e15
Open Access | Times Cited: 338
Impact of GPCR Structures on Drug Discovery
Miles Congreve, Chris de Graaf, Nigel A. Swain, et al.
Cell (2020) Vol. 181, Iss. 1, pp. 81-91
Open Access | Times Cited: 299
5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology
Yao Peng, John D. McCorvy, Kasper Harpsøe, et al.
Cell (2018) Vol. 172, Iss. 4, pp. 719-730.e14
Open Access | Times Cited: 210
Structural insights into the human D1 and D2 dopamine receptor signaling complexes
Youwen Zhuang, Peiyu Xu, Chunyou Mao, et al.
Cell (2021) Vol. 184, Iss. 4, pp. 931-942.e18
Open Access | Times Cited: 195
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
Structure of a D2 dopamine receptor–G-protein complex in a lipid membrane
Jie Yin, Kuang-Yui Michael Chen, Mary J. Clark, et al.
Nature (2020) Vol. 584, Iss. 7819, pp. 125-129
Open Access | Times Cited: 173
Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes
Peng Xiao, Wei Yan, Lu Gou, et al.
Cell (2021) Vol. 184, Iss. 4, pp. 943-956.e18
Open Access | Times Cited: 122
Structure-Based Virtual Screening for Ligands of G Protein–Coupled Receptors: What Can Molecular Docking Do for You?
Flavio Ballante, Albert J. Kooistra, Stefanie Kampen, et al.
Pharmacological Reviews (2021) Vol. 73, Iss. 4, pp. 1698-1736
Open Access | Times Cited: 104
Structure-based discovery of nonopioid analgesics acting through the α 2A -adrenergic receptor
Elissa A. Fink, Jun Xu, Harald Hübner, et al.
Science (2022) Vol. 377, Iss. 6614
Open Access | Times Cited: 101
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
Structural basis of ligand recognition and self-activation of orphan GPR52
Xi Lin, Mingyue Li, Niandong Wang, et al.
Nature (2020) Vol. 579, Iss. 7797, pp. 152-157
Closed Access | Times Cited: 127
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
Property-Unmatched Decoys in Docking Benchmarks
Reed M. Stein, Yang Ying, Trent E. Balius, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 2, pp. 699-714
Open Access | Times Cited: 93
Haloperidol bound D2 dopamine receptor structure inspired the discovery of subtype selective ligands
Luyu Fan, Liang Tan, Zhangcheng Chen, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 92
VEGAS as a Platform for Facile Directed Evolution in Mammalian Cells
Justin G. English, Reid H. J. Olsen, Katherine Lansu, et al.
Cell (2019) Vol. 178, Iss. 3, pp. 748-761.e17
Open Access | Times Cited: 91
Crystal structures of the human neurokinin 1 receptor in complex with clinically used antagonists
Jendrik Schöppe, Janosch Ehrenmann, Christoph Klenk, et al.
Nature Communications (2018) Vol. 10, Iss. 1
Open Access | Times Cited: 89
Biased ligands at opioid receptors: Current status and future directions
Tao Che, Hemlata Dwivedi‐Agnihotri, Arun K. Shukla, et al.
Science Signaling (2021) Vol. 14, Iss. 677
Open Access | Times Cited: 86
Structures of the human dopamine D3 receptor-Gi complexes
Peiyu Xu, Sijie Huang, Chunyou Mao, et al.
Molecular Cell (2021) Vol. 81, Iss. 6, pp. 1147-1159.e4
Open Access | Times Cited: 71
Highlighting membrane protein structure and function: A celebration of the Protein Data Bank
Fei Li, Pascal F. Egea, Alex J. Vecchio, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100557-100557
Open Access | Times Cited: 58
Nonantimicrobial Actions of Macrolides: Overview and Perspectives for Future Development
Jennifer Kricker, Clive P. Page, Fridrik Runar Gardarsson, et al.
Pharmacological Reviews (2021) Vol. 73, Iss. 4, pp. 1404-1433
Open Access | Times Cited: 58
“Selective” serotonin 5-HT2A receptor antagonists
Austen B. Casey, Meng Cui, Raymond G. Booth, et al.
Biochemical Pharmacology (2022) Vol. 200, pp. 115028-115028
Open Access | Times Cited: 52
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