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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:

Allosteric Binding Sites of the SARS-CoV-2 Main Protease: Potential Targets for Broad-Spectrum Anti-Coronavirus Agents
Lara Alzyoud, Mohammad A. Ghattas, Noor Atatreh
Drug Design Development and Therapy (2022) Vol. Volume 16, pp. 2463-2478
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

A Comprehensive Review of the Clinical Pharmacokinetics, Pharmacodynamics, and Drug Interactions of Nirmatrelvir/Ritonavir
Jacqueline G. Gerhart, Donna S. Cox, Ravi Shankar Prasad Singh, et al.
Clinical Pharmacokinetics (2024) Vol. 63, Iss. 1, pp. 27-42
Open Access | Times Cited: 20
Structural and Mechanistic Insights into the Main Protease (Mpro) Dimer Interface Destabilization Inhibitor: Unveiling New Therapeutic Avenues against SARS-CoV-2
Ankur Singh, Kuldeep Jangid, Sanketkumar Nehul, et al.
Biochemistry (2025)
Closed Access | Times Cited: 1
Dynamical Nonequilibrium Molecular Dynamics Simulations Identify Allosteric Sites and Positions Associated with Drug Resistance in the SARS-CoV-2 Main Protease
H. T. Henry Chan, A. Sofia F. Oliveira, Christopher J. Schofield, et al.
JACS Au (2023) Vol. 3, Iss. 6, pp. 1767-1774
Open Access | Times Cited: 26
SARS-CoV-2 Mpro Inhibitors: Achieved Diversity, Developing Resistance and Future Strategies
Conrad Fischer, Jenson R. Feys
Future Pharmacology (2023) Vol. 3, Iss. 1, pp. 80-107
Open Access | Times Cited: 24
Green and efficient one-pot three-component synthesis of novel drug-like furo[2,3-d]pyrimidines as potential active site inhibitors and putative allosteric hotspots modulators of both SARS-CoV-2 MPro and PLPro
Hossein Mousavi, Behzad Zeynizadeh, Mehdi Rimaz
Bioorganic Chemistry (2023) Vol. 135, pp. 106390-106390
Open Access | Times Cited: 24
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: 22
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: 19
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
Unveiling the mechanism of action of a novel natural dual inhibitor of SARS-CoV-2 Mpro and PLpro with molecular dynamics simulations
Xiaoxia Gu, Xiaotian Zhang, Xueke Zhang, et al.
Natural Products and Bioprospecting (2025) Vol. 15, Iss. 1
Open Access
Dihydropyrimidine-2-thione derivatives as SARS-CoV-2 main protease inhibitors: synthesis, SAR and in vitro profiling
Anees Saeed, Ayesha Tahir, Muhammad Shah, et al.
RSC Advances (2025) Vol. 15, Iss. 8, pp. 6424-6440
Open Access
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: 14
Long Time Scale Ensemble Methods in Molecular Dynamics: Ligand–Protein Interactions and Allostery in SARS-CoV-2 Targets
Agastya P. Bhati, Art Hoti, Andrew Potterton, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 11, pp. 3359-3378
Open Access | Times Cited: 11
Computational investigation on the antioxidant activities and on the Mpro SARS-CoV-2 non-covalent inhibition of isorhamnetin
Maciej Spiegel, Giada Ciardullo, Tiziana Marino, et al.
Frontiers in Chemistry (2023) Vol. 11
Open Access | Times Cited: 10
An allosteric mechanism for potent inhibition of SARS-CoV-2 main proteinase
Yunju Zhang, Jingjing Guo, Yang Liu, et al.
International Journal of Biological Macromolecules (2024) Vol. 265, pp. 130644-130644
Closed Access | Times Cited: 3
Discovery of Meisoindigo derivatives as noncovalent and orally available Mpro inhibitors: their therapeutic implications in the treatment of COVID-19
Qingtian Gao, Sixu Liu, Yuzheng Zhou, et al.
European Journal of Medicinal Chemistry (2024) Vol. 273, pp. 116498-116498
Closed Access | Times Cited: 3
3C-like proteases in SARS-CoV-2
Kenana Al Adem, Juliana C. Ferreira, Adrian J. Villanueva, et al.
Bioscience Reports (2024)
Open Access | Times Cited: 2
Structural review of SARS-CoV-2 antiviral targets
Wen Cui, Yinkai Duan, Gao Yan, et al.
Structure (2024) Vol. 32, Iss. 9, pp. 1301-1321
Closed Access | Times Cited: 2
Inhibition of the predicted allosteric site of the SARS-CoV-2 main protease through flavonoids
Bibi Kubra, Syed Badshah, Shah Faisal, et al.
Journal of Biomolecular Structure and Dynamics (2022) Vol. 41, Iss. 18, pp. 9103-9120
Closed Access | Times Cited: 10
Structural and thermodynamic properties of conserved water molecules in Mpro native: A combined approach by MD simulation and Grid Inhomogeneous Solvation Theory
Hridoy R. Bairagya, Alvea Tasneem, Debapriyo Sarmadhikari
Proteins Structure Function and Bioinformatics (2024) Vol. 92, Iss. 6, pp. 735-749
Closed Access | Times Cited: 1
Mechanistic Insights into the Mutational Landscape of the Main Protease/3CLPro and Its Impact on Long-Term COVID-19/SARS-CoV-2 Management
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonjabulo Ntombikhona Magwaza, et al.
(2024)
Open Access | Times Cited: 1
A potential allosteric inhibitor of SARS-CoV-2 main protease (Mpro) identified through metastable state analysis
Asma Fatima, Anupriya M. Geethakumari, Wesam S. Ahmed, et al.
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 1
The Discovery of Novel Small Oxindole‐Based Inhibitors Targeting the SARS‐CoV‐2 Main Protease (Mpro)
Lara Alzyoud, Radwa E. Mahgoub, Feda E. Mohamed, et al.
Chemistry & Biodiversity (2023) Vol. 20, Iss. 11
Open Access | Times Cited: 4
Docking-Based Evidence for the Potential of ImmunoDefender: A Novel Formulated Essential Oil Blend Incorporating Synergistic Antiviral Bioactive Compounds as Promising Mpro Inhibitors against SARS-CoV-2
Ayoub Ksouri, Anis Klouz, Balkiss Bouhaouala‐Zahar, et al.
Molecules (2023) Vol. 28, Iss. 11, pp. 4296-4296
Open Access | Times Cited: 3
Discovery of Novel Cysteine Protease Inhibitors for the Treatment of Coronavirus (COVID-19)
Surya K. De
Current Medicinal Chemistry (2023) Vol. 31, Iss. 9, pp. 1165-1169
Closed Access | Times Cited: 2
Discovery of Novel SARS-CoV-2 3CLpro Inhibitors from Natural Products by FRET-Based Assay
Tianyu Zhang, Jixia Wang, Xianlong Ye, et al.
(2024)
Closed Access
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