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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:

Structural basis for replicase polyprotein cleavage and substrate specificity of main protease from SARS-CoV-2
Yao Zhao, Yan Zhu, Xiang Liu, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 16
Open Access | Times Cited: 130

Showing 1-25 of 130 citing articles:

Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors
Seyed Arad Moghadasi, Emmanuel Heilmann, Ahmed Magdy Khalil, et al.
Science Advances (2023) Vol. 9, Iss. 13
Open Access | Times Cited: 134
Molecular mechanisms of SARS-CoV-2 resistance to nirmatrelvir
Yinkai Duan, Hao Zhou, Xiang Liu, et al.
Nature (2023) Vol. 622, Iss. 7982, pp. 376-382
Closed Access | Times Cited: 105
X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation
Jaeyong Lee, Calem Kenward, L.J. Worrall, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 67
Functional map of SARS-CoV-2 3CL protease reveals tolerant and immutable sites
Sho Iketani, Seo Jung Hong, Jenny Sheng, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 10, pp. 1354-1362.e6
Open Access | Times Cited: 50
Structural biology of SARS-CoV-2 Mpro and drug discovery
Yinkai Duan, Haofeng Wang, Zhenghong Yuan, et al.
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102667-102667
Closed Access | Times Cited: 24
Virtual Screening of Peptide Libraries: The Search for Peptide-Based Therapeutics Using Computational Tools
Marian Vincenzi, Flavia Anna Mercurio, Marilisa Leone
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 3, pp. 1798-1798
Open Access | Times Cited: 16
Artificial urinary biomarker probes for diagnosis
Cheng Xu, Kanyi Pu
Nature Reviews Bioengineering (2024) Vol. 2, Iss. 5, pp. 425-441
Closed Access | Times Cited: 13
Structure-based design of pan-coronavirus inhibitors targeting host cathepsin L and calpain-1
Xiong Xie, Qiaoshuai Lan, Jinyi Zhao, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 12
Transformative Approaches in SARS-CoV-2 Management: Vaccines, Therapeutics and Future Direction
Ankita Saha, Shweta Choudhary, Priyanshu Walia, et al.
Virology (2025) Vol. 604, pp. 110394-110394
Closed Access | Times Cited: 1
Distal protein-protein interactions contribute to nirmatrelvir resistance
Eric M. Lewandowski, Xiujun Zhang, Haozhou Tan, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors
Seyed Arad Moghadasi, Emmanuel Heilmann, Ahmed Magdy Khalil, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 31
Medicinal chemistry strategies towards the development of non-covalent SARS-CoV-2 Mpro inhibitors
Letian Song, Shenghua Gao, Bing Ye, et al.
Acta Pharmaceutica Sinica B (2023) Vol. 14, Iss. 1, pp. 87-109
Open Access | Times Cited: 21
The NSP4 T492I mutation increases SARS-CoV-2 infectivity by altering non-structural protein cleavage
Xiaoyuan Lin, Zhou Sha, Jakob Trimpert, et al.
Cell Host & Microbe (2023) Vol. 31, Iss. 7, pp. 1170-1184.e7
Open Access | Times Cited: 19
SARS-CoV-2 polyprotein substrate regulates the stepwise Mpro cleavage reaction
M. Narwal, Jean‐Paul Armache, Thomas J. Edwards, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 5, pp. 104697-104697
Open Access | Times Cited: 18
Non-peptidic inhibitors targeting SARS-CoV-2 main protease: A review
Ya-Qi Xiao, Jiao Long, Shuang‐Shuang Zhang, et al.
Bioorganic Chemistry (2024) Vol. 147, pp. 107380-107380
Closed Access | Times Cited: 8
Discovery and Crystallographic Studies of Nonpeptidic Piperazine Derivatives as Covalent SARS-CoV-2 Main Protease Inhibitors
Shenghua Gao, Letian Song, Tobias Claff, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 24, pp. 16902-16917
Closed Access | Times Cited: 25
An in-solution snapshot of SARS-COV-2 main protease maturation process and inhibition
G.D. Noske, Yun Song, R.S. Fernandes, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Key allosteric and active site residues of SARS-CoV-2 3CLpro are promising drug targets
Kenana Al Adem, Juliana C. Ferreira, Samar Fadl, et al.
Biochemical Journal (2023) Vol. 480, Iss. 11, pp. 791-813
Open Access | Times Cited: 15
Danshensu inhibits SARS-CoV-2 by targeting its main protease as a specific covalent inhibitor and discovery of bifunctional compounds eliciting antiviral and anti-inflammatory activity
Ruyu Wang, Xuwen Chen, Hongtao Li, et al.
International Journal of Biological Macromolecules (2023) Vol. 257, pp. 128623-128623
Closed Access | Times Cited: 15
Lessons Learnt from COVID-19: Computational Strategies for Facing Present and Future Pandemics
Matteo Pavan, Stefano Moro
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 5, pp. 4401-4401
Open Access | Times Cited: 14
Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 Main Protease using a linked protein FRET platform
Calem Kenward, M. Vuckovic, Mark Paetzel, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107367-107367
Open Access | Times Cited: 6
Computational evaluation and benchmark study of 342 crystallographic holo-structures of SARS-CoV-2 Mpro enzyme
Hamlet Khachatryan, Mher Matevosyan, Vardan Harutyunyan, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 6
SARS-CoV-2 NSP5 antagonizes MHC II expression by subverting histone deacetylase 2
Nima Taefehshokr, Alex Lac, Angela M. Vrieze, et al.
Journal of Cell Science (2024) Vol. 137, Iss. 10
Open Access | Times Cited: 5
Covalent small-molecule inhibitors of SARS-CoV-2 Mpro: Insights into their design, classification, biological activity, and binding interactions
Ahmed M. Shawky, Faisal A. Almalki, Hayat Ali Alzahrani, et al.
European Journal of Medicinal Chemistry (2024) Vol. 277, pp. 116704-116704
Closed Access | Times Cited: 5
Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro
Ruchi Yadav, Valentine V. Courouble, Sanjay Kumar Dey, et al.
Science Advances (2022) Vol. 8, Iss. 49
Open Access | Times Cited: 21
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