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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:

Penicillin Derivatives Inhibit the SARS-CoV-2 Main Protease by Reaction with Its Nucleophilic Cysteine
Tika R. Malla, Lennart Brewitz, Dorian-Gabriel Muntean, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 11, pp. 7682-7696
Open Access | Times Cited: 32

Showing 1-25 of 32 citing articles:

Therapeutic strategies for COVID-19: progress and lessons learned
Guangdi Li, Rolf Hilgenfeld, Richard J. Whitley, et al.
Nature Reviews Drug Discovery (2023) Vol. 22, Iss. 6, pp. 449-475
Open Access | Times Cited: 420
The research progress of SARS-CoV-2 main protease inhibitors from 2020 to 2022
Xiaojing Pang, Wei Xu, Yang Liu, et al.
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115491-115491
Open Access | Times Cited: 63
Structure and function of SARS-CoV and SARS-CoV-2 main proteases and their inhibition: A comprehensive review
Xin Li, Yongcheng Song
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115772-115772
Open Access | Times Cited: 52
Alkyne Derivatives of SARS-CoV-2 Main Protease Inhibitors Including Nirmatrelvir Inhibit by Reacting Covalently with the Nucleophilic Cysteine
Lennart Brewitz, Leo Dumjahn, Yilin Zhao, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 4, pp. 2663-2680
Open Access | Times Cited: 50
COVID-19 therapeutics: Small-molecule drug development targeting SARS-CoV-2 main protease
Thales Kronenberger, Stefan Laufer, Thanigaimalai Pillaiyar
Drug Discovery Today (2023) Vol. 28, Iss. 6, pp. 103579-103579
Open Access | Times Cited: 43
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: 23
Cyclic β2,3-amino acids improve the serum stability of macrocyclic peptide inhibitors targeting the SARS-CoV-2 main protease
Takashi Miura, Tika R. Malla, Lennart Brewitz, et al.
Bulletin of the Chemical Society of Japan (2024) Vol. 97, Iss. 5
Open Access | Times Cited: 11
On the origins of SARS-CoV-2 main protease inhibitors
Yves L. Janin
RSC Medicinal Chemistry (2023) Vol. 15, Iss. 1, pp. 81-118
Closed Access | Times Cited: 17
Advances in research on 3C-like protease (3CLpro) inhibitors against SARS-CoV-2 since 2020
Roufen Chen, Yali Gao, Han Liu, et al.
RSC Medicinal Chemistry (2022) Vol. 14, Iss. 1, pp. 9-21
Open Access | Times Cited: 26
Discovery of highly potent covalent SARS-CoV-2 3CLpro inhibitors bearing 2-sulfoxyl-1,3,4-oxadiazole scaffold for combating COVID-19
Fu-Mao Zhang, Ting Huang, Feng Wang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115721-115721
Closed Access | Times Cited: 13
Discovery and Mechanism Study of SARS-CoV-2 3C-like Protease Inhibitors with a New Reactive Group
Pengxuan Ren, Hui Li, Tianqing Nie, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 17, pp. 12266-12283
Closed Access | Times Cited: 13
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: 5
Nanozymes with Modulable Inhibition Transfer Pathways for Thiol and Cell Identification
Lijun Hu, Lei Jiao, Chengjie Chen, et al.
Analytical Chemistry (2025)
Closed Access
In Silico Discovery of SARS-CoV-2 Main Protease Inhibitors Using Docking, Molecular Dynamics, and Fragment Molecular Orbital Calculations
Takeshi Ishikawa, Kenji Matsumoto, Toshiyuki Hamada, et al.
The Journal of Physical Chemistry B (2025) Vol. 129, Iss. 6, pp. 1740-1749
Closed Access
Silaproline-bearing nirmatrelvir derivatives are potent inhibitors of the SARS-CoV-2 main protease highlighting the value of silicon-derivatives in structure-activity-relationship studies
Dóra Laczi, Sofia Schönbauer Huamán, Taylah Andrews-Clark, et al.
European Journal of Medicinal Chemistry (2025), pp. 117603-117603
Open Access
Structure-guided design of direct-acting antivirals that exploit the gem-dimethyl effect and potently inhibit 3CL proteases of severe acute respiratory syndrome Coronavirus-2 (SARS-CoV-2) and middle east respiratory syndrome coronavirus (MERS-CoV)
Chamandi S. Dampalla, Matthew J. Miller, Yunjeong Kim, et al.
European Journal of Medicinal Chemistry (2023) Vol. 254, pp. 115376-115376
Open Access | Times Cited: 10
Thiophene-fused γ-lactams inhibit the SARS-CoV-2 main protease via reversible covalent acylation
Gayatri Tehlan, Lennart Brewitz, Lewis T. Ibbotson, et al.
Chemical Science (2024) Vol. 15, Iss. 20, pp. 7667-7678
Open Access | Times Cited: 3
Covalent binding of withanolides to cysteines of protein targets
Christian Bailly
Biochemical Pharmacology (2024) Vol. 226, pp. 116405-116405
Open Access | Times Cited: 3
Design, Synthesis, and Antiviral Activity of Fragmented-Lapatinib Aminoquinazoline Analogs towards SARS-CoV-2 Inhibition
Ayomide Adediji, Akeanan Sroithongmoon, Aphinya Suroengrit, et al.
European Journal of Medicinal Chemistry (2025), pp. 117303-117303
Closed Access
Discovery, synthesis and mechanism study of 2,3,5-substituted [1,2,4]-thiadiazoles as covalent inhibitors targeting 3C-Like protease of SARS-CoV-2
Pengxuan Ren, Changyue Yu, Ruxue Zhang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 249, pp. 115129-115129
Open Access | Times Cited: 8
Targeting SARS-CoV-2 Main Protease: A Successful Story Guided by an In Silico Drug Repurposing Approach
Francesca Alessandra Ambrosio, Giosuè Costa, Isabella Romeo, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 11, pp. 3601-3613
Open Access | Times Cited: 6
Computational analysis of substrate recognition of Sars-Cov-2 Mpro main protease
Hilal Sena Tasci, Ebru Akkus, Müslüm Yıldız, et al.
Computational Biology and Chemistry (2023) Vol. 107, pp. 107960-107960
Closed Access | Times Cited: 6
αβ,α′β′-Diepoxyketones are mechanism-based inhibitors of nucleophilic cysteine enzymes
Mariska de Munnik, J. D. Lithgow, Lennart Brewitz, et al.
Chemical Communications (2023) Vol. 59, Iss. 86, pp. 12859-12862
Open Access | Times Cited: 4
Methods for production and assaying catalysis of isolated recombinant human aspartate/asparagine-β-hydroxylase
Lennart Brewitz, Amelia Brasnett, Lara I. Schnaubelt, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 313-344
Closed Access | Times Cited: 1
A review on recent theoretical approaches made in the discovery of potential Covid-19 therapeutics
Apurba K. Bhattacharjee
Journal of Mathematical Chemistry (2024) Vol. 62, Iss. 10, pp. 2924-2942
Closed Access | Times Cited: 1
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