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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:

Preclinical characterization of an intravenous coronavirus 3CL protease inhibitor for the potential treatment of COVID19
Britton Boras, Rhys Jones, Brandon J. Anson, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 261

Showing 26-50 of 261 citing articles:

Therapeutics for COVID-19
Sima S. Toussi, Jennifer Hammond, Brian S. Gerstenberger, et al.
Nature Microbiology (2023) Vol. 8, Iss. 5, pp. 771-786
Open Access | Times Cited: 66
Bench-to-bedside: Innovation of small molecule anti-SARS-CoV-2 drugs in China
Liyan Yang, Zhonglei Wang
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115503-115503
Open Access | Times Cited: 63
Development of Highly Potent Noncovalent Inhibitors of SARS-CoV-2 3CLpro
Ningke Hou, Lei Shuai, Lijing Zhang, et al.
ACS Central Science (2023) Vol. 9, Iss. 2, pp. 217-227
Open Access | Times Cited: 60
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: 51
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: 46
An update on the discovery and development of reversible covalent inhibitors
Faridoon Faridoon, Raymond Ng, Guiping Zhang, et al.
Medicinal Chemistry Research (2023) Vol. 32, Iss. 6, pp. 1039-1062
Open Access | Times Cited: 41
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: 40
In vitro and in vivo characterization of SARS-CoV-2 resistance to ensitrelvir
Maki Kiso, Seiya Yamayoshi, Shun Iida, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 39
Preclinical evaluation of the SARS-CoV-2 Mpro inhibitor RAY1216 shows improved pharmacokinetics compared with nirmatrelvir
Xiaoxin Chen, Xiaodong Huang, Qinhai Ma, et al.
Nature Microbiology (2024) Vol. 9, Iss. 4, pp. 1075-1088
Open Access | Times Cited: 28
COVID-19 drug discovery and treatment options
Jasper Fuk‐Woo Chan, Shuofeng Yuan, Hin Chu, et al.
Nature Reviews Microbiology (2024) Vol. 22, Iss. 7, pp. 391-407
Closed Access | Times Cited: 17
Perspectives on SARS-CoV-2 Main Protease Inhibitors
Kaifu Gao, Rui Wang, Jiahui Chen, et al.
Journal of Medicinal Chemistry (2021) Vol. 64, Iss. 23, pp. 16922-16955
Open Access | Times Cited: 93
Discovery and Crystallographic Studies of Trisubstituted Piperazine Derivatives as Non-Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity and Low Toxicity
Shenghua Gao, Katharina Sylvester, Letian Song, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 19, pp. 13343-13364
Closed Access | Times Cited: 63
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
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: 61
Remdesivir-induced emergence of SARS-CoV2 variants in patients with prolonged infection
Andreas Heyer, Thomas Günther, Alexis Robitaille, et al.
Cell Reports Medicine (2022) Vol. 3, Iss. 9, pp. 100735-100735
Open Access | Times Cited: 55
Nirmatrelvir plus ritonavir (Paxlovid) a potent SARS-CoV-2 3CLpro protease inhibitor combination
Jordi Reina, Carla Iglesias
Revista Española de Quimioterapia (2022) Vol. 35, Iss. 3, pp. 236-240
Open Access | Times Cited: 49
Antiviral cyclic peptides targeting the main protease of SARS-CoV-2
Jason Johansen‐Leete, Sven Ullrich, Sarah E. Fry, et al.
Chemical Science (2022) Vol. 13, Iss. 13, pp. 3826-3836
Open Access | Times Cited: 48
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
Validation and Invalidation of SARS-CoV-2 Papain-like Protease Inhibitors
Chunlong Ma, Jun Wang
ACS Pharmacology & Translational Science (2022) Vol. 5, Iss. 2, pp. 102-109
Open Access | Times Cited: 45
Small‐Molecule Quenchers for Förster Resonance Energy Transfer: Structure, Mechanism, and Applications
Bin Fang, Yu Shen, Bo Peng, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 41
Closed Access | Times Cited: 43
The substitutions L50F, E166A and L167F in SARS-CoV-2 3CLpro are selected by a protease inhibitorin vitroand confer resistance to nirmatrelvir
Dirk Jochmans, Liu C, Kim Donckers, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 42
Recent Advances in PROTACs for Drug Targeted Protein Research
Tingting Yao, Heng Xiao, Hong Wang, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 18, pp. 10328-10328
Open Access | Times Cited: 41
Comparative evaluation of authorized drugs for treating Covid‐19 patients
Towhidul Islam, Moynul Hasan, Mohammad Saydur Rahman, et al.
Health Science Reports (2022) Vol. 5, Iss. 4
Open Access | Times Cited: 38
Resistance to nirmatrelvir due to mutations in the Mpro in the subvariants of SARS-CoV-2 Omicron: Another concern?
Srijan Chatterjee, Manojit Bhattacharya, Kuldeep Dhama, et al.
Molecular Therapy — Nucleic Acids (2023) Vol. 32, pp. 263-266
Open Access | Times Cited: 26
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: 24

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