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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 new generation Mpro inhibitor with potent activity against SARS-CoV-2 Omicron variants
Chong Huang, Huiping Shuai, Jingxin Qiao, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 54

Showing 1-25 of 54 citing articles:

Structure and function of SARS-CoV and SARS-CoV-2 main proteases and their inhibition: A comprehensive review
Xin Li, Yongcheng Song
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115772-115772
Open Access | Times Cited: 52
Molecular mechanism of ensitrelvir inhibiting SARS-CoV-2 main protease and its variants
Meng-Meng Lin, Xudong Zeng, Yinkai Duan, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 36
Recent Advances in SARS-CoV-2 Main Protease Inhibitors: From Nirmatrelvir to Future Perspectives
Andrea Citarella, Alessandro Dimasi, Davide Moi, et al.
Biomolecules (2023) Vol. 13, Iss. 9, pp. 1339-1339
Open Access | Times Cited: 28
An orally bioavailable SARS-CoV-2 main protease inhibitor exhibits improved affinity and reduced sensitivity to mutations
Michael Westberg, Yichi Su, Xinzhi Zou, et al.
Science Translational Medicine (2024) Vol. 16, Iss. 738
Open Access | Times Cited: 13
Contributions of Hyperactive Mutations in Mpro from SARS-CoV-2 to Drug Resistance
Julia M. Flynn, Sarah N. Zvornicanin, Tenzin Tsepal, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 4, pp. 1174-1184
Closed Access | Times Cited: 9
Inhibitors of SARS-CoV-2 Main Protease (Mpro) as Anti-Coronavirus Agents
Agnieszka Zagórska, Anna Czopek, Monika Fryc, et al.
Biomolecules (2024) Vol. 14, Iss. 7, pp. 797-797
Open Access | Times Cited: 9
On the origins of SARS-CoV-2 main protease inhibitors
Yves L. Janin
RSC Medicinal Chemistry (2023) Vol. 15, Iss. 1, pp. 81-118
Closed Access | Times Cited: 17
Progress in Research on Inhibitors Targeting SARS-CoV-2 Main Protease (Mpro)
Yue Yang, Yidan Luo, Chenbo Zhang, et al.
ACS Omega (2024) Vol. 9, Iss. 32, pp. 34196-34219
Open Access | Times Cited: 6
Recent Advances on SARS-CoV-2 Mpro Inhibitors: From Nirmatrelvir to Future Perspectives
Andrea Citarella, Alessandro Dimasi, Davide Moi, et al.
(2023)
Open Access | Times Cited: 14
SARS-CoV-2 Mpro oligomerization as a potential target for therapy
Kinga Lis, Jacek Plewka, Filipe Menezes, et al.
International Journal of Biological Macromolecules (2024) Vol. 267, pp. 131392-131392
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
Discovery of Nirmatrelvir Resistance Mutations in SARS-CoV-2 3CLpro: A Computational-Experimental Approach
Brandon Havranek, Robel Demissie, Hyun Lee, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 22, pp. 7180-7188
Open Access | Times Cited: 11
Nonpeptidic Irreversible Inhibitors of SARS-CoV-2 Main Protease with Potent Antiviral Activity
Angelo Oneto, Ghazl Al Hamwi, Laura Schäkel, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 17, pp. 14986-15011
Closed Access | Times Cited: 4
Design, Synthesis, and Unprecedented Interactions of Covalent Dipeptide-Based Inhibitors of SARS-CoV-2 Main Protease and Its Variants Displaying Potent Antiviral Activity
Philipp Flury, Nadine Krüger, Katharina Sylvester, et al.
Journal of Medicinal Chemistry (2025)
Closed Access
A Tale of Two Drugs: Molnupiravir and Paxlovid
Michael D. Waters, Stafford G. Warren
Mutation Research/Reviews in Mutation Research (2025) Vol. 795, pp. 108533-108533
Closed Access
Navigating COVID-19: advancements in therapeutics and viral filtration technologies for Today's challenges and tomorrow's solutions
Devesh U. Kapoor, Bhavna Kumar, Manmohan Singhal, et al.
Journal of Drug Delivery Science and Technology (2025), pp. 106741-106741
Closed Access
Design, synthesis and activity evaluation of 4-(quinoline-2-yl)aniline derivatives as SARS-CoV‑2 main protease inhibitors
Honglei Bao, Hui Meng, Shilin Gong, et al.
Bioorganic & Medicinal Chemistry (2025) Vol. 121, pp. 118135-118135
Closed Access
Determination of SARS-CoV-2 Main Protease (Mpro) Activity Based on Electrooxidation of Tyrosine Residue of a Model Peptide
Tatiana A. Filippova, Rami A. Masamrekh, Tatiana Farafonova, et al.
Biochemistry (Moscow) (2025) Vol. 90, Iss. 1, pp. 120-131
Closed Access
Research progress on critical viral protease inhibitors for coronaviruses and enteroviruses
Shulei Hu, Qiuyu Zhong, Xiong Xie, et al.
Bioorganic & Medicinal Chemistry Letters (2025), pp. 130168-130168
Closed Access
Inhibitory efficacy and structural insights of Bofutrelvir against SARS-CoV-2 Mpro mutants and MERS-CoV Mpro
Weiwei Wang, Xuelan Zhou, Wen Li, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access
A deep learning model for structure-based bioactivity optimization and its application in the bioactivity optimization of a SARS-CoV-2 main protease inhibitor
Zhenyu Yang, Kai Wang, Guo Zhang, et al.
European Journal of Medicinal Chemistry (2025), pp. 117602-117602
Closed Access
Investigation of the Interaction Between 4‐Thiazolidinone Derivatives and SARS‐CoV‐2 Mpro Using Spectroscopy and Microscale Thermophoresis
Leyao Chen, N. Wang, Xiaoyu Chang, et al.
ChemistrySelect (2025) Vol. 10, Iss. 15
Closed Access
Structure-based discovery of highly bioavailable, covalent, broad-spectrum coronavirus M Pro inhibitors with potent in vivo efficacy
Tyler C. Detomasi, Gilles Degotte, Sijie Huang, et al.
Science Advances (2025) Vol. 11, Iss. 17
Open Access
Harnessing Brazilian biodiversity database: identification of flavonoids as potential inhibitors of SARS-CoV-2 main protease using computational approaches and all-atom molecular dynamics simulation
João Augusto Pereira da Rocha, Renato Araújo da Costa, Andréia do Socorro Silva da Costa, et al.
Frontiers in Chemistry (2024) Vol. 12
Open Access | Times Cited: 3
Macrocyclic Azapeptide Nitriles: Structure-Based Discovery of Potent SARS-CoV-2 Main Protease Inhibitors as Antiviral Drugs
Julian Breidenbach, Rabea Voget, Yaoyao Si, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 11, pp. 8757-8790
Closed Access | Times Cited: 3
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