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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:

Impact of Early Pandemic Stage Mutations on Molecular Dynamics of SARS-CoV-2 Mpro
Olivier Sheik Amamuddy, Gennady M. Verkhivker, Özlem Taştan Bishop
Journal of Chemical Information and Modeling (2020) Vol. 60, Iss. 10, pp. 5080-5102
Open Access | Times Cited: 83

Showing 1-25 of 83 citing articles:

Targeting SARS-CoV-2 Proteases for COVID-19 Antiviral Development
Zongyang Lv, Kristin E. Cano, Lijia Jia, et al.
Frontiers in Chemistry (2022) Vol. 9
Open Access | Times Cited: 75
Accelerating COVID-19 Research Using Molecular Dynamics Simulation
Aditya K. Padhi, Soumya Lipsa Rath, Timir Tripathi
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 32, pp. 9078-9091
Closed Access | Times Cited: 66
Potential Resistance of SARS-CoV-2 Main Protease (Mpro) against Protease Inhibitors: Lessons Learned from HIV-1 Protease
János András Mótyán, Mohamed Mahdi, Gyula Hoffka, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3507-3507
Open Access | Times Cited: 61
TRIM7 inhibits enterovirus replication and promotes emergence of a viral variant with increased pathogenicity
Wenchun Fan, Katrina B. Mar, Levent Sari, et al.
Cell (2021) Vol. 184, Iss. 13, pp. 3410-3425.e17
Open Access | Times Cited: 60
Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2
Kaifu Gao, Rui Wang, Jiahui Chen, et al.
Chemical Reviews (2022) Vol. 122, Iss. 13, pp. 11287-11368
Open Access | Times Cited: 58
Genomic Variations in the Structural Proteins of SARS-CoV-2 and Their Deleterious Impact on Pathogenesis: A Comparative Genomics Approach
Taj Mohammad, Arunabh Choudhury, Insan Habib, et al.
Frontiers in Cellular and Infection Microbiology (2021) Vol. 11
Open Access | Times Cited: 58
MD simulations indicate Omicron P132H of SARS-CoV-2 Mpro is a potential allosteric mutant involved in modulating the dynamics of catalytic site entry loop
Zahoor Ahmad Bhat, Mohd Muzammil Khan, Ayyub Rehman, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130077-130077
Closed Access | Times Cited: 7
Lead Discovery of SARS-CoV-2 Main Protease Inhibitors through Covalent Docking-Based Virtual Screening
Giorgio Amendola, Roberta Ettari, Santo Previti, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 4, pp. 2062-2073
Closed Access | Times Cited: 47
Molecular docking and dynamics study to explore phytochemical ligand molecules against the main protease of SARS-CoV-2 from extensive phytochemical datasets
Shafi Mahmud, Mohasana Akter Mita, Suvro Biswas, et al.
Expert Review of Clinical Pharmacology (2021) Vol. 14, Iss. 10, pp. 1305-1315
Closed Access | Times Cited: 44
Ligand-based design, synthesis, computational insights, andin vitrostudies of novelN-(5-Nitrothiazol-2-yl)-carboxamido derivatives as potent inhibitors of SARS-CoV-2 main protease
Mohamed Elagawany, Ayman Abo Elmaaty, Ahmed Mostafa, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2022) Vol. 37, Iss. 1, pp. 2112-2132
Open Access | Times Cited: 35
Insights into SARS-CoV-2 structure: Approaches and action of SARS-CoV-2 main protease inhibitor
Ilma Shakeel, Aaliya Taiyab, Aanchal Rathi, et al.
Elsevier eBooks (2025), pp. 89-117
Closed Access
Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease
Thomas J. Cross, Gemma R. Takahashi, Elizabeth M. Diessner, et al.
Biochemistry (2020) Vol. 59, Iss. 39, pp. 3741-3756
Open Access | Times Cited: 43
Identification of mutation resistance coldspots for targeting the SARS‐CoV2 main protease
Navaneethakrishnan Krishnamoorthy, Khalid A. Fakhro
IUBMB Life (2021) Vol. 73, Iss. 4, pp. 670-675
Open Access | Times Cited: 39
Repurposing of FDA‐approved drugs against active site and potential allosteric drug‐binding sites of COVID‐19 main protease
Merve Yuce, Erdem Cicek, Tuğçe İnan, et al.
Proteins Structure Function and Bioinformatics (2021) Vol. 89, Iss. 11, pp. 1425-1441
Open Access | Times Cited: 39
Extracting Dynamical Correlations and Identifying Key Residues for Allosteric Communication in Proteins by correlationplus
Mustafa Tekpinar, Bertrand Néron, Marc Delarue
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 10, pp. 4832-4838
Open Access | Times Cited: 38
Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing
Serdar Durdağı, Çağdaş Dağ, Berna Doğan, et al.
Structure (2021) Vol. 29, Iss. 12, pp. 1382-1396.e6
Open Access | Times Cited: 36
Biochemical features and mutations of key proteins in SARS-CoV-2 and their impacts on RNA therapeutics
Li Zeng, Dongying Li, Weida Tong, et al.
Biochemical Pharmacology (2021) Vol. 189, pp. 114424-114424
Open Access | Times Cited: 35
MDM-TASK-web: MD-TASK and MODE-TASK web server for analyzing protein dynamics
Olivier Sheik Amamuddy, Michael Glenister, Thulani Tshabalala, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 5059-5071
Open Access | Times Cited: 33
Molecular dynamics of the viral life cycle: progress and prospects
Peter Eugene Jones, Carolina Pérez-Segura, Alexander J. Bryer, et al.
Current Opinion in Virology (2021) Vol. 50, pp. 128-138
Open Access | Times Cited: 28
Allosteric Hotspots in the Main Protease of SARS-CoV-2
Léonie Strömich, Nan Wu, Mauricio Barahona, et al.
Journal of Molecular Biology (2022) Vol. 434, Iss. 17, pp. 167748-167748
Open Access | Times Cited: 18
Antiviral activities of natural compounds and ionic liquids to inhibit the Mpro of SARS-CoV-2: a computational approach
Kandhan Palanisamy, S. M. Esther Rubavathy, Muthuramalingam Prakash, et al.
RSC Advances (2022) Vol. 12, Iss. 6, pp. 3687-3695
Open Access | Times Cited: 17
Dynamic allostery highlights the evolutionary differences between the CoV-1 and CoV-2 main proteases
Paul Campitelli, Lu Jin, S. Banu Ozkan
Biophysical Journal (2022) Vol. 121, Iss. 8, pp. 1483-1492
Open Access | Times Cited: 17
Novel dynamic residue network analysis approaches to study allosteric modulation: SARS-CoV-2 Mpro and its evolutionary mutations as a case study
Olivier Sheik Amamuddy, Rita Afriyie Boateng, Victor Barozi, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 6431-6455
Open Access | Times Cited: 20
Deciphering Isoniazid Drug Resistance Mechanisms on Dimeric Mycobacterium tuberculosis KatG via Post-molecular Dynamics Analyses Including Combined Dynamic Residue Network Metrics
Victor Barozi, Thommas M. Musyoka, Olivier Sheik Amamuddy, et al.
ACS Omega (2022) Vol. 7, Iss. 15, pp. 13313-13332
Open Access | Times Cited: 14
Allostery and Missense Mutations as Intermittently Linked Promising Aspects of Modern Computational Drug Discovery
Özlem Taştan Bishop, Thommas M. Musyoka, Victor Barozi
Journal of Molecular Biology (2022) Vol. 434, Iss. 17, pp. 167610-167610
Open Access | Times Cited: 14
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