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:

Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease
Elizabeth A. MacDonald, Gary Frey, Mark Namchuk, et al.
ACS Infectious Diseases (2021) Vol. 7, Iss. 9, pp. 2591-2595
Open Access | Times Cited: 73

Showing 26-50 of 73 citing articles:

High-Resolution Substrate Specificity Profiling of SARS-CoV-2 Mpro; Comparison to SARS-CoV Mpro
Rasha M. Yaghi, Collin L. Andrews, Dennis Wylie, et al.
ACS Chemical Biology (2024) Vol. 19, Iss. 7, pp. 1474-1483
Open Access | Times Cited: 4

A new inactive conformation of SARS-CoV-2 main protease
Emanuele Fornasier, Maria Ludovica Macchia, Gabriele Giachin, et al.
Acta Crystallographica Section D Structural Biology (2022) Vol. 78, Iss. 3, pp. 363-378
Open Access | Times Cited: 19

Recognition and cleavage of human tRNA methyltransferase TRMT1 by the SARS-CoV-2 main protease
Angel D′Oliviera, Xiangyu Dai, Saba Mottaghinia, et al.
eLife (2025) Vol. 12
Open Access

Optimization of SARS-CoV-2 Mpro Inhibitors by a Structure-Based Multilevel Virtual Screening Method
Lanlan Jing, Fabao Zhao, Lin Zheng, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 2, pp. 670-670
Open Access

Identification of novel and potent inhibitors of SARS-CoV-2 main protease from DNA-encoded chemical libraries
Dario Akaberi, Monireh Pourghasemi Lati, Janina Krambrich, et al.
Antimicrobial Agents and Chemotherapy (2024) Vol. 68, Iss. 10
Open Access | Times Cited: 3

Allostery in homodimeric SARS-CoV-2 main protease
Emanuele Fornasier, Simone Fabbian, Haidi Shehi, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 3

Recognition and Cleavage of Human tRNA Methyltransferase TRMT1 by the SARS-CoV-2 Main Protease
Angel D′Oliviera, Xuhang Dai, Saba Mottaghinia, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 8

Studies on the selectivity of the SARS-CoV-2 papain-like protease reveal the importance of the P2′ proline of the viral polyprotein
H. T. Henry Chan, Lennart Brewitz, Petra Lukacik, et al.
RSC Chemical Biology (2023) Vol. 5, Iss. 2, pp. 117-130
Open Access | Times Cited: 6

Unsupervised deep learning for molecular dynamics simulations: a novel analysis of protein–ligand interactions in SARS-CoV-2 Mpro
Jessica Mustali, Ikki Yasuda, Yoshinori Hirano, et al.
RSC Advances (2023) Vol. 13, Iss. 48, pp. 34249-34261
Open Access | Times Cited: 5

How viral proteins bind short linear motifs and intrinsically disordered domains
Priyanka Madhu, Norman E. Davey, Ylva Ivarsson
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 935-944
Closed Access | Times Cited: 9

Analyzing 3D structures of the SARS-CoV-2 main protease reveals structural features of ligand binding for COVID-19 drug discovery
Liang Xu, Ru Chen, Jie Liu, et al.
Drug Discovery Today (2023) Vol. 28, Iss. 10, pp. 103727-103727
Closed Access | Times Cited: 5

The Inhibitory Potential of Ferulic Acid Derivatives against the SARS-CoV-2 Main Protease: Molecular Docking, Molecular Dynamics, and ADMET Evaluation
Io Antonopoulou, Eleftheria Sapountzaki, Ulrika Rova, et al.
Biomedicines (2022) Vol. 10, Iss. 8, pp. 1787-1787
Open Access | Times Cited: 7

Binding and Unbinding Pathways of Peptide Substrates on the SARS-CoV-2 3CL Protease
Kei Moritsugu, Toru Ekimoto, Mitsunori Ikeguchi, et al.
Journal of Chemical Information and Modeling (2022) Vol. 63, Iss. 1, pp. 240-250
Closed Access | Times Cited: 7

Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors
Andrey Kovalevsky, Annie Aniana, Rodolfo Ghirlando, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 20, pp. 18478-18490
Closed Access | Times Cited: 1

Sunflower Trypsin Monocyclic Inhibitor Selected for the Main Protease of SARS-CoV-2 by Phage Display
Graziele Cristina Ferreira, Verônica de Moraes Manzato, Débora Noma Okamoto, et al.
Biological and Pharmaceutical Bulletin (2024) Vol. 47, Iss. 11, pp. 1813-1822
Open Access | Times Cited: 1

Recognition and Cleavage of Human tRNA Methyltransferase TRMT1 by the SARS-CoV-2 Main Protease
Angel D′Oliviera, Xuhang Dai, Saba Mottaghinia, et al.
(2024)
Open Access | Times Cited: 1

Catalytic Mechanism of SARS-CoV-2 3-Chymotrypsin-Like Protease as Determined by Steady-State and Pre-Steady-State Kinetics
Jiyun Zhu, A. Kemp, Balachandra Chenna, et al.
ACS Catalysis (2024) Vol. 14, Iss. 24, pp. 18292-18309
Open Access | Times Cited: 1

Prediction and validation of host cleavage targets of SARS-CoV-2 3C-like protease
Nora Yucel, Silvia Marchianò, Evan Tchelepi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

Defining the Substrate Envelope of SARS-CoV-2 Main Protease to Predict and Avoid Drug Resistance
Ala M. Shaqra, Sarah N. Zvornicanin, Qiu Yu J. Huang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

Inhibition of Cysteine Proteases via Thiol-Michael Addition Explains the Anti-SARS-CoV-2 and Bioactive Properties of Arteannuin B
Kaitlyn Varela, Hadi D. Arman, Mitchel S. Berger, et al.
Journal of Natural Products (2023) Vol. 86, Iss. 7, pp. 1654-1666
Closed Access | Times Cited: 3

Coronaviral Main Protease Induces LPCAT3 Cleavage and Endoplasmic Reticulum (ER) Stress
Jia Wang, Meifang Zhang, Yanli Ding, et al.
Viruses (2023) Vol. 15, Iss. 8, pp. 1696-1696
Open Access | Times Cited: 3

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