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:

Dynamic Profiling of β-Coronavirus 3CL Mpro Protease Ligand-Binding Sites
Eunice Cho, Margarida Rosa, Ruhi Anjum, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 6, pp. 3058-3073
Open Access | Times Cited: 48

Showing 1-25 of 48 citing articles:

Targeting SARS-CoV-2 Main Protease for Treatment of COVID-19: Covalent Inhibitors Structure–Activity Relationship Insights and Evolution Perspectives
Gabriele La Monica, Alessia Bono, Antonino Lauria, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 19, pp. 12500-12534
Open Access | Times Cited: 98

Comprehensive fitness landscape of SARS-CoV-2 Mpro reveals insights into viral resistance mechanisms
Julia M. Flynn, Neha S. Samant, Gily Schneider-Nachum, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 97

Olgotrelvir, a dual inhibitor of SARS-CoV-2 Mpro and cathepsin L, as a standalone antiviral oral intervention candidate for COVID-19
Long Mao, Namir Shaabani, Xiaoying Zhang, et al.
Med (2024) Vol. 5, Iss. 1, pp. 42-61.e23
Open Access | Times Cited: 17

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: 70

Functional map of SARS-CoV-2 3CL protease reveals tolerant and immutable sites
Sho Iketani, Seo Jung Hong, Jenny Sheng, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 10, pp. 1354-1362.e6
Open Access | Times Cited: 48

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: 25

An in-solution snapshot of SARS-COV-2 main protease maturation process and inhibition
G.D. Noske, Yun Song, R.S. Fernandes, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15

Investigating the inhibition of benzimidazole derivatives on SARS-CoV-2 M pro by enzyme activity inhibition, spectroscopy, and molecular docking
Xueyuan Wang, Leyao Chen, Xiaoyu Chang, et al.
Journal of Biomolecular Structure and Dynamics (2025), pp. 1-16
Closed Access

Decoding SARS‐CoV‐2 Inhibition: Insights From Molecular Dynamics Simulation of Condensed Amino Thiourea Scaffold Small Molecules
Xiaoli Shen, Hao Zhang, Pengyin Zhang, et al.
Journal of Cellular Biochemistry (2025) Vol. 126, Iss. 2
Closed Access

SARSCoV‐2 Mpro Dihedral Angles Reveal Allosteric Signaling
Daniel J. Evans, Samreen Sheraz, Albert Y. Lau
Proteins Structure Function and Bioinformatics (2025)
Closed Access

Conserved coronavirus proteins as targets of broad-spectrum antivirals
Cleber C. Melo‐Filho, Tesia Bobrowski, Holli‐Joi Martin, et al.
Antiviral Research (2022) Vol. 204, pp. 105360-105360
Open Access | Times Cited: 26

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

Covalent small-molecule inhibitors of SARS-CoV-2 Mpro: Insights into their design, classification, biological activity, and binding interactions
Ahmed M. Shawky, Faisal A. Almalki, Hayat Ali Alzahrani, et al.
European Journal of Medicinal Chemistry (2024) Vol. 277, pp. 116704-116704
Closed Access | Times Cited: 4

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: 3

Development of de-novo coronavirus 3-chymotrypsin-like protease (3CLpro) inhibitors since COVID-19 outbreak: A strategy to tackle challenges of persistent virus infection
Lei Tian, Taotao Qiang, Xiuding Yang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 264, pp. 115979-115979
Closed Access | Times Cited: 9

Computational Identification of Possible Allosteric Sites and Modulators of the SARS-CoV-2 Main Protease
Debarati DasGupta, Wallace Chan, Heather A. Carlson
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 3, pp. 618-626
Open Access | Times Cited: 14

Hydroxamate and thiosemicarbazone: Two highly promising scaffolds for the development of SARS-CoV-2 antivirals
Yin‐Sui Xu, Jia‐Zhu Chigan, Jiaqi Li, et al.
Bioorganic Chemistry (2022) Vol. 124, pp. 105799-105799
Open Access | Times Cited: 14

Deciphering the Coevolutionary Dynamics of L2 β-Lactamases via Deep Learning
Yu Zhu, Jing Gu, Zhuoran Zhao, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 9, pp. 3706-3717
Open Access | Times Cited: 2

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 insights into the substrate‐binding site of main protease for the structure‐based COVID‐19 drug discovery
Rohoullah Firouzi, Mitra Ashouri, Mohammad Hossein Karimi‐Jafari
Proteins Structure Function and Bioinformatics (2022) Vol. 90, Iss. 5, pp. 1090-1101
Closed Access | Times Cited: 13

Machine learning prediction of 3CL SARS-CoV-2 docking scores
Lukáš Bučinský, Dušan Bortňák, Marián Gall, et al.
Computational Biology and Chemistry (2022) Vol. 98, pp. 107656-107656
Open Access | Times Cited: 11

Adaptive language model training for molecular design
Andrew E. Blanchard, Debsindhu Bhowmik, Zachary Fox, et al.
Journal of Cheminformatics (2023) Vol. 15, Iss. 1
Open Access | Times Cited: 6

Repositioning of anti-dengue compounds against SARS-CoV-2 as viral polyprotein processing inhibitor
Leena H. Bajrai, Arwa A. Faizo, Areej Alkhaldy, et al.
PLoS ONE (2022) Vol. 17, Iss. 11, pp. e0277328-e0277328
Open Access | Times Cited: 10

In Silico Design of New Dual Inhibitors of SARS-CoV-2 MPRO through Ligand- and Structure-Based Methods
Alessia Bono, Antonino Lauria, Gabriele La Monica, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 9, pp. 8377-8377
Open Access | Times Cited: 5

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