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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:

Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease
A. Douangamath, D. Fearon, Paul Gehrtz, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 486

Showing 26-50 of 486 citing articles:

Crystal Structure of SARS-CoV-2 Main Protease in Complex with the Non-Covalent Inhibitor ML188
G.J. Lockbaum, Archie C. Reyes, Jeong Min Lee, et al.
Viruses (2021) Vol. 13, Iss. 2, pp. 174-174
Open Access | Times Cited: 96
Fragment-to-Lead Medicinal Chemistry Publications in 2020
Iwan J. P. de Esch, Daniel A. Erlanson, Wolfgang Jahnke, et al.
Journal of Medicinal Chemistry (2021) Vol. 65, Iss. 1, pp. 84-99
Open Access | Times Cited: 82
Repurposing drugs for the management of COVID-19
Jacopo Cusinato, Ylenia Cau, Anna Maria Calvani, et al.
Expert Opinion on Therapeutic Patents (2020) Vol. 31, Iss. 4, pp. 295-307
Closed Access | Times Cited: 76
Exploring the Druggability of Conserved RNA Regulatory Elements in the SARS‐CoV‐2 Genome
Sridhar Sreeramulu, Christian Richter, Hannes Berg, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 35, pp. 19191-19200
Open Access | Times Cited: 75
An automatic pipeline for the design of irreversible derivatives identifies a potent SARS-CoV-2 Mpro inhibitor
Daniel Zaidman, Paul Gehrtz, Mihajlo Filep, et al.
Cell chemical biology (2021) Vol. 28, Iss. 12, pp. 1795-1806.e5
Open Access | Times Cited: 73
Discovery of SARS-CoV-2 Mpro peptide inhibitors from modelling substrate and ligand binding
H. T. Henry Chan, Marc A. Moesser, Rebecca K. Walters, et al.
Chemical Science (2021) Vol. 12, Iss. 41, pp. 13686-13703
Open Access | Times Cited: 73
Unveiling the molecular mechanism of SARS-CoV-2 main protease inhibition from 137 crystal structures using algebraic topology and deep learning
Duc Duy Nguyen, Kaifu Gao, Jiahui Chen, et al.
Chemical Science (2020) Vol. 11, Iss. 44, pp. 12036-12046
Open Access | Times Cited: 72
Identification of natural compounds as potent inhibitors of SARS-CoV-2 main protease using combined docking and molecular dynamics simulations
Deeba Shamim Jairajpuri, Afzal Hussain, Khalida Nasreen, et al.
Saudi Journal of Biological Sciences (2021) Vol. 28, Iss. 4, pp. 2423-2431
Open Access | Times Cited: 71
DeepFrag: a deep convolutional neural network for fragment-based lead optimization
Harrison Green, David Ryan Koes, Jacob D. Durrant
Chemical Science (2021) Vol. 12, Iss. 23, pp. 8036-8047
Open Access | Times Cited: 69
Target 2035 – update on the quest for a probe for every protein
Susanne Müller, Suzanne Ackloo, Arij Al Chawaf, et al.
RSC Medicinal Chemistry (2021) Vol. 13, Iss. 1, pp. 13-21
Open Access | Times Cited: 69
X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation
Jaeyong Lee, Calem Kenward, L.J. Worrall, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 66
A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process
G.D. Noske, A.M. Nakamura, Victor O. Gawriljuk, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 18, pp. 167118-167118
Open Access | Times Cited: 65
A structural view of the SARS-CoV-2 virus and its assembly
Nathan Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
Discovery of chebulagic acid and punicalagin as novel allosteric inhibitors of SARS-CoV-2 3CLpro
Ruikun Du, Laura Cooper, Zinuo Chen, et al.
Antiviral Research (2021) Vol. 190, pp. 105075-105075
Open Access | Times Cited: 60
Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source
A. Douangamath, A.J. Powell, D. Fearon, et al.
Journal of Visualized Experiments (2021), Iss. 171
Open Access | Times Cited: 60
The battle between host and SARS-CoV-2: Innate immunity and viral evasion strategies
Shilei Zhang, Lulan Wang, Genhong Cheng
Molecular Therapy (2022) Vol. 30, Iss. 5, pp. 1869-1884
Open Access | Times Cited: 60
Non-covalent SARS-CoV-2 Mpro inhibitors developed from in silico screen hits
Giacomo G. Rossetti, Marianna Ossorio, S. Rempel, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 60
A Comprehensive Review about the Molecular Structure of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2): Insights into Natural Products against COVID-19
Essa M. Saied, Yousra A. El‐Maradny, Alaa A. Osman, et al.
Pharmaceutics (2021) Vol. 13, Iss. 11, pp. 1759-1759
Open Access | Times Cited: 58
Covalent Warheads Targeting Cysteine Residue: The Promising Approach in Drug Development
Fangjiao Huang, Xiaoli Han, Xiaohui Xiao, et al.
Molecules (2022) Vol. 27, Iss. 22, pp. 7728-7728
Open Access | Times Cited: 58
Small-Molecule Thioesters as SARS-CoV-2 Main Protease Inhibitors: Enzyme Inhibition, Structure–Activity Relationships, Antiviral Activity, and X-ray Structure Determination
Thanigaimalai Pillaiyar, Philipp Flury, Nadine Krüger, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 13, pp. 9376-9395
Closed Access | Times Cited: 57
Automated discovery of noncovalent inhibitors of SARS-CoV-2 main protease by consensus Deep Docking of 40 billion small molecules
Francesco Gentile, Michael Fernández, Fuqiang Ban, et al.
Chemical Science (2021) Vol. 12, Iss. 48, pp. 15960-15974
Open Access | Times Cited: 56
Key dimer interface residues impact the catalytic activity of 3CLpro, the main protease of SARS-CoV-2
Juliana C. Ferreira, Samar Fadl, Wael M. Rabeh
Journal of Biological Chemistry (2022) Vol. 298, Iss. 6, pp. 102023-102023
Open Access | Times Cited: 44
xia2.multiplex: a multi-crystal data-analysis pipeline
Richard J. Gildea, James Beilsten‐Edmands, Danny Axford, et al.
Acta Crystallographica Section D Structural Biology (2022) Vol. 78, Iss. 6, pp. 752-769
Open Access | Times Cited: 44
A Multistage In Silico Study of Natural Potential Inhibitors Targeting SARS-CoV-2 Main Protease
Eslam B. Elkaeed, Ibrahim H. Eissa, Hazem Elkady, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 15, pp. 8407-8407
Open Access | Times Cited: 44
The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro)
Ali Ebrahim, Blake T. Riley, D. Kumaran, et al.
IUCrJ (2022) Vol. 9, Iss. 5, pp. 682-694
Open Access | Times Cited: 44

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