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:

Design, synthesis and in vitro evaluation of novel SARS-CoV-2 3CLpro covalent inhibitors
Julia Stille, Jevgenijs Tjutrins, Guanyu Wang, et al.
European Journal of Medicinal Chemistry (2021) Vol. 229, pp. 114046-114046
Open Access | Times Cited: 62

Showing 1-25 of 62 citing articles:

The SARS‐CoV‐2 main protease (Mpro): Structure, function, and emerging therapies for COVID‐19
Qing Hu, Yuan Xiong, Guanghao Zhu, et al.
MedComm (2022) Vol. 3, Iss. 3
Open Access | Times Cited: 148

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: 101

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

SARS-CoV-2 Main Protease Drug Design, Assay Development, and Drug Resistance Studies
Bin Tan, Ryan Joyce, Haozhou Tan, et al.
Accounts of Chemical Research (2022) Vol. 56, Iss. 2, pp. 157-168
Open Access | Times Cited: 62

Advances in the Development of SARS-CoV-2 Mpro Inhibitors
Laura Agost-Beltrán, Sergio de la Hoz‐Rodríguez, Lledó Bou‐Iserte, et al.
Molecules (2022) Vol. 27, Iss. 8, pp. 2523-2523
Open Access | Times Cited: 54

Recent Advances in SARS-CoV-2 Main Protease Inhibitors: From Nirmatrelvir to Future Perspectives
Andrea Citarella, Alessandro Dimasi, Davide Moi, et al.
Biomolecules (2023) Vol. 13, Iss. 9, pp. 1339-1339
Open Access | Times Cited: 28

SARS-CoV-2 Mpro Inhibitors: Achieved Diversity, Developing Resistance and Future Strategies
Conrad Fischer, Jenson R. Feys
Future Pharmacology (2023) Vol. 3, Iss. 1, pp. 80-107
Open Access | Times Cited: 25

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

Molecular Interactions of Tannic Acid with Proteins Associated with SARS-CoV-2 Infectivity
Mohamed Haddad, Roger Gaudreault, Gabriel Sasseville, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 5, pp. 2643-2643
Open Access | Times Cited: 34

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

Exploring diverse reactive warheads for the design of SARS-CoV-2 main protease inhibitors
Bin Tan, M. Sacco, Haozhou Tan, et al.
European Journal of Medicinal Chemistry (2023) Vol. 259, pp. 115667-115667
Open Access | Times Cited: 20

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

Photocatalytic redox-neutral α-C(sp3)–H pyridination of glycine derivatives and N-arylamines with cyanopyridines
Changduo Pan, Dongdong Chen, Yangjian Cheng, et al.
Chemical Communications (2024) Vol. 60, Iss. 33, pp. 4451-4454
Closed Access | Times Cited: 6

Progress in Research on Inhibitors Targeting SARS-CoV-2 Main Protease (Mpro)
Yue Yang, Yidan Luo, Chenbo Zhang, et al.
ACS Omega (2024) Vol. 9, Iss. 32, pp. 34196-34219
Open Access | Times Cited: 6

Sulforaphane is a reversible covalent inhibitor of 3‐chymotrypsin‐like protease of SARS‐CoV‐2
Zinuo Chen, Ruikun Du, Laura Cooper, et al.
Journal of Medical Virology (2023) Vol. 95, Iss. 3
Closed Access | Times Cited: 14

Recent Advances on SARS-CoV-2 Mpro Inhibitors: From Nirmatrelvir to Future Perspectives
Andrea Citarella, Alessandro Dimasi, Davide Moi, et al.
(2023)
Open Access | Times Cited: 14

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

Design, Synthesis, X-ray Crystallography, and Biological Activities of Covalent, Non-Peptidic Inhibitors of SARS-CoV-2 Main Protease
Md Ashraf-Uz-Zaman, Teck Khiang Chua, Xin Li, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 2, pp. 715-731
Closed Access | Times Cited: 5

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

In silico screening-based discovery of novel covalent inhibitors of the SARS-CoV-2 3CL protease
Muya Xiong, Tianqing Nie, Qiang Shao, et al.
European Journal of Medicinal Chemistry (2022) Vol. 231, pp. 114130-114130
Open Access | Times Cited: 21

MasitinibL shows promise as a drug-like analog of masitinib that elicits comparable SARS-Cov-2 3CLpro inhibition with low kinase preference
Olanrewaju Ayodeji Durojaye, Nkwachukwu Oziamara Okoro, Arome Solomon Odiba, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 11

Identification of promising SARS-CoV-2 main protease inhibitor through molecular docking, dynamics simulation, and ADMET analysis
Ganesh Sharma, Neeraj Kumar, Chandra Shekhar Sharma, et al.
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access

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