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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:

A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs
Debajit Dey, Enya Qing, Yanan He, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9

Showing 9 citing articles:

Production and cryo-electron microscopy structure of an internally tagged SARS-CoV-2 spike ecto-domain construct
Suruchi Singh, Yi Liu, Meghan C. Burke, et al.
Journal of Structural Biology X (2025) Vol. 11, pp. 100123-100123
Open Access
Sequences in the Cytoplasmic Tail Contribute to the Intracellular Trafficking and the Cell Surface Localization of SARS-CoV-2 Spike Protein
Evgeniya E. Burkova, Irina A. Bakhno
Biomolecules (2025) Vol. 15, Iss. 2, pp. 280-280
Open Access
Identification of three novel B cell epitopes targeting the bovine viral diarrhea virus NS3 protein for use in diagnostics and vaccine development
Yuanyuan Zhang, Jing Cheng, Wenxiao Liu, et al.
International Journal of Biological Macromolecules (2025), pp. 142767-142767
Closed Access
SARS-CoV-2 hijacks a cell damage response, which induces transcription of a more efficient Spike S-acyltransferase
Francisco S. Mesquita, Laurence Abrami, Lucie Bracq, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 4
Strengths and limitations of SARS-CoV-2 virus-like particle systems
Rokaia Sultana, Robert V. Stahelin
Virology (2024) Vol. 601, pp. 110285-110285
Open Access | Times Cited: 1
SARS-CoV-2 Omicron variations reveal mechanisms controlling cell entry dynamics and antibody neutralization
Enya Qing, Julisa Salgado, Alexandria Wilcox, et al.
PLoS Pathogens (2024) Vol. 20, Iss. 12, pp. e1012757-e1012757
Open Access | Times Cited: 1
Evidence that the SARS-CoV-2 S protein undergoes a conformational change at the Golgi Complex that leads to the formation of virus neutralising antibody binding epitopes in the S1 protein subunit.
Richard J. Sugrue, Boon Huan Tan, Soak Kuan Lai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Dimming the corona: studying SARS-coronavirus-2 at reduced biocontainment level using replicons and virus-like particles
Grace Neilsen, Asha Maria Mathew, J.M. Castro, et al.
mBio (2024)
Open Access
Evidence that the SARS-CoV-2 S protein undergoes a conformational change at the Golgi complex that leads to the formation of virus neutralising antibody binding epitopes in the S1 protein subunit
Yanjun Wu, Soak Kuan Lai, Conrad En-Zuo Chan, et al.
Virology (2024) Vol. 598, pp. 110187-110187
Open Access
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