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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 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

Showing 19 citing articles:

Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations
Sheikh Bilal Ahmad, Maria Batool, Quratul Ain, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 17, pp. 9124-9124
Open Access | Times Cited: 109
Qualitative Estimation of Protein–Ligand Complex Stability through Thermal Titration Molecular Dynamics Simulations
Matteo Pavan, Silvia Menin, Davide Bassani, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 22, pp. 5715-5728
Open Access | Times Cited: 42
Protein structure-based in-silico approaches to drug discovery: Guide to COVID-19 therapeutics
Yash Gupta, Oleksandr V. Savytskyi, Matt Coban, et al.
Molecular Aspects of Medicine (2022) Vol. 91, pp. 101151-101151
Open Access | Times Cited: 30
Thermal Titration Molecular Dynamics (TTMD): Not Your Usual Post-Docking Refinement
Silvia Menin, Matteo Pavan, Veronica Salmaso, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3596-3596
Open Access | Times Cited: 21
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: 20
From the Wuhan-Hu-1 strain to the XD and XE variants: is targeting the SARS-CoV-2 spike protein still a pharmaceutically relevant option against COVID-19?
Matteo Pavan, Davide Bassani, Mattia Sturlese, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2022) Vol. 37, Iss. 1, pp. 1704-1714
Open Access | Times Cited: 23
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: 13
In-silico investigation of phenolic compounds from leaves of Phillyrea angustifolia L. as a potential inhibitor against the SARS-CoV-2 main protease (Mpro PDB ID:5R83) using a virtual screening method
Ahmed Boufissiou, Mohnad Abdalla, Mohamed Sharaf, et al.
Journal of Saudi Chemical Society (2022) Vol. 26, Iss. 3, pp. 101473-101473
Open Access | Times Cited: 20
Frustration in physiology and molecular medicine
R. Gonzalo Parra, Elizabeth A. Komives, Peter G. Wolynes, et al.
Molecular Aspects of Medicine (2025) Vol. 103, pp. 101362-101362
Open Access
A comprehensive study of SARS-CoV-2 mfigain protease (Mpro) inhibitor-resistant mutants selected in a VSV-based system
Francesco Costacurta, Andrea Dodaro, David Bante, et al.
PLoS Pathogens (2024) Vol. 20, Iss. 9, pp. e1012522-e1012522
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
Targeting the I7L Protease: A Rational Design for Anti-Monkeypox Drugs?
Andrea Dodaro, Matteo Pavan, Stefano Moro
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 8, pp. 7119-7119
Open Access | Times Cited: 8
A comprehensive study of SARS-CoV-2 main protease (Mpro) inhibitor-resistant mutants selected in a VSV-based system
Francesco Costacurta, Andrea Dodaro, David Bante, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 8
On Inactivation of the Coronavirus Main Protease
Hong Ha Nguyen, Jim Tufts, David D. L. Minh
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 5, pp. 1644-1656
Closed 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
Dimeric and monomeric conformation of SARS-CoV-2 main protease: New technical approaches based on IR radiation
Federica Piccirilli, Hendrik Vondracek, Lucia Silvestrini, et al.
Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy (2024) Vol. 322, pp. 124772-124772
Open Access | Times Cited: 1
Bat coronaviruses related to SARS-CoV-2: what about their 3CL proteases (MPro)?
Matteo Pavan, Davide Bassani, Mattia Sturlese, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2022) Vol. 37, Iss. 1, pp. 1077-1082
Open Access | Times Cited: 4
Molecular Docking, ADMET Analysis and Molecular Dynamics (MD) Simulation to Identify Synthetic Isoquinolines as Potential Inhibitors of SARS-CoV-2 MPRO
Paulo Ricardo dos Santos Correia, Alesson Henrique Donato de Souza, Andrés Reyes‐Chaparro, et al.
Current Computer - Aided Drug Design (2023) Vol. 19, Iss. 5, pp. 391-404
Closed Access | Times Cited: 1
In Silico Insights Toward the Exploration of Adenosine Receptors Ligand Recognition
Davide Bassani, Stefano Moro
Topics in medicinal chemistry (2023), pp. 275-315
Closed Access
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