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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:

Structure-guided discovery of a single-domain antibody agonist against human apelin receptor
Yanbin Ma, Yao Ding, Xianqiang Song, et al.
Science Advances (2020) Vol. 6, Iss. 3
Open Access | Times Cited: 72

Showing 1-25 of 72 citing articles:

Ig-VAE: Generative modeling of protein structure by direct 3D coordinate generation
Raphael R. Eguchi, Christian A. Choe, Po‐Ssu Huang
PLoS Computational Biology (2022) Vol. 18, Iss. 6, pp. e1010271-e1010271
Open Access | Times Cited: 90
Structure-based design of non-hypertrophic apelin receptor modulator
Weiwei Wang, Su‐Yu Ji, W. Zhang, et al.
Cell (2024) Vol. 187, Iss. 6, pp. 1460-1475.e20
Closed Access | Times Cited: 17
Exploring cellular biochemistry with nanobodies
Ross W. Cheloha, Thibault J. Harmand, Charlotte Wijne, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 45, pp. 15307-15327
Open Access | Times Cited: 82
SYNBIP: synthetic binding proteins for research, diagnosis and therapy
Xiaona Wang, Fengcheng Li, Wenqi Qiu, et al.
Nucleic Acids Research (2021) Vol. 50, Iss. D1, pp. D560-D570
Open Access | Times Cited: 64
Structure of the core human NADPH oxidase NOX2
Sigrid Noreng, Naruhisa Ota, Yonglian Sun, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 51
Structural insight into apelin receptor-G protein stoichiometry
Yue Yang, Lier Liu, Lijie Wu, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 7, pp. 688-697
Closed Access | Times Cited: 38
Structural basis of α1A-adrenergic receptor activation and recognition by an extracellular nanobody
Yosuke Toyoda, Angqi Zhu, Fang Kong, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
Antibodies expand the scope of angiotensin receptor pharmacology
Meredith A. Skiba, Sarah M. Sterling, Shaun Rawson, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 12, pp. 1577-1585
Closed Access | Times Cited: 12
Structural insights into the regulation of monomeric and dimeric apelin receptor
Yue Yang, Lier Liu, Lijie Wu, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
De novodesign of miniprotein agonists and antagonists targeting G protein-coupled receptors
Edin Muratspahić, David Feldman, David E. Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access | Times Cited: 1
Membrane protein production and formulation for drug discovery
Ellen Gulezian, Christina Crivello, Janna Bednenko, et al.
Trends in Pharmacological Sciences (2021) Vol. 42, Iss. 8, pp. 657-674
Closed Access | Times Cited: 47
Accelerating GPCR Drug Discovery With Conformation-Stabilizing VHHs
Toon Laeremans, Zara A. Sands, Pieter Claes, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 33
Nanobody-based sensors reveal a high proportion of mGlu heterodimers in the brain
Jiyong Meng, Chanjuan Xu, Pierre‐André Lafon, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 894-903
Open Access | Times Cited: 33
Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8
Dawei Sun, Yonglian Sun, Eric M. Janezic, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 17
Highly biased agonism for GPCR ligands via nanobody tethering
Shivani Sachdev, Brendan A. Creemer, Thomas J. Gardella, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Structural insights into CXCR4 modulation and oligomerization
Kei Saotome, Luke L. McGoldrick, Jo-Hao Ho, et al.
Nature Structural & Molecular Biology (2024)
Open Access | Times Cited: 6
Structural basis of μ-opioid receptor targeting by a nanobody antagonist
Jun Yu, Amit Kumar, Xuefeng Zhang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Synthetic nanobodies as angiotensin receptor blockers
Conor McMahon, Dean P. Staus, Laura M. Wingler, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 33, pp. 20284-20291
Open Access | Times Cited: 44
Ig-VAE: Generative Modeling of Protein Structure by Direct 3D Coordinate Generation
Raphael R. Eguchi, Christian A. Choe, Po‐Ssu Huang
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 42
Structure–function relationship and physiological role of apelin and its G protein coupled receptor
Subhashree Murali, Gopala Krishna Aradhyam
Biophysical Reviews (2023) Vol. 15, Iss. 1, pp. 127-143
Open Access | Times Cited: 14
Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain
Arum Wu, David Salom, John D. Hong, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14
Structural insights into CXCR4 modulation and oligomerization
Kei Saotome, Luke L. McGoldrick, Jo-Hao Ho, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Structural basis for selectivity and antagonism in extracellular GPCR-nanobodies
Roman R. Schlimgen, Francis C. Peterson, Raimond Heukers, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Structure elucidation of a human melanocortin-4 receptor specific orthosteric nanobody agonist
Thomas D. Fontaine, Andreas Büsch, Toon Laeremans, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Advancements in the conservation of the conformational epitope of membrane protein immunogens
Aisha Mahboob, Nishat Fatma, Faraz Ahmed, et al.
Frontiers in Immunology (2025) Vol. 16
Open Access
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