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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 1-25 of 261 citing articles:

Crystal structure of SARS-CoV-2 main protease in complex with protease inhibitor PF-07321332
Yao Zhao, Chao Fang, Qi Zhang, et al.
Protein & Cell (2021) Vol. 13, Iss. 9, pp. 689-693
Open Access | Times Cited: 207
Naturally Occurring Mutations of SARS-CoV-2 Main Protease Confer Drug Resistance to Nirmatrelvir
Yanmei Hu, Eric M. Lewandowski, Haozhou Tan, et al.
ACS Central Science (2023) Vol. 9, Iss. 8, pp. 1658-1669
Open Access | Times Cited: 204
Defining the risk of SARS-CoV-2 variants on immune protection
Marciela M. DeGrace, Elodie Ghedin, Matthew B. Frieman, et al.
Nature (2022) Vol. 605, Iss. 7911, pp. 640-652
Open Access | Times Cited: 152
Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants
S.E. Greasley, Stephen Noell, Olga Plotnikova, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 6, pp. 101972-101972
Open Access | Times Cited: 147
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: 144
Considerations for the discovery and development of 3-chymotrypsin-like cysteine protease inhibitors targeting SARS-CoV-2 infection
Koen Vandyck, Jérôme Deval
Current Opinion in Virology (2021) Vol. 49, pp. 36-40
Open Access | Times Cited: 129
The Substitutions L50F, E166A, and L167F in SARS-CoV-2 3CLpro Are Selected by a Protease Inhibitor In Vitro and Confer Resistance To Nirmatrelvir
Dirk Jochmans, Liu C, Kim Donckers, et al.
mBio (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 127
Accurate prediction of molecular properties and drug targets using a self-supervised image representation learning framework
Xiangxiang Zeng, Hongxin Xiang, Linhui Yu, et al.
Nature Machine Intelligence (2022) Vol. 4, Iss. 11, pp. 1004-1016
Open Access | Times Cited: 126
Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors
Seyed Arad Moghadasi, Emmanuel Heilmann, Ahmed Magdy Khalil, et al.
Science Advances (2023) Vol. 9, Iss. 13
Open Access | Times Cited: 126
Discovery of Di- and Trihaloacetamides as Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity
Chunlong Ma, Zilei Xia, M. Sacco, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 49, pp. 20697-20709
Open Access | Times Cited: 121
Progress and Challenges in Targeting the SARS-CoV-2 Papain-like Protease
Haozhou Tan, Yanmei Hu, Prakash D. Jadhav, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 11, pp. 7561-7580
Open Access | Times Cited: 115
The oral protease inhibitor (PF-07321332) protects Syrian hamsters against infection with SARS-CoV-2 variants of concern
Rana Abdelnabi, Caroline S. Foo, Dirk Jochmans, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 112
Molnupiravir and Its Antiviral Activity Against COVID-19
Lili Tian, Zehan Pang, Maochen Li, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 102
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: 99
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease
Daniel W. Kneller, Hui Li, G.N. Phillips, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 96
Accelerating antiviral drug discovery: lessons from COVID-19
Annette von Delft, Matthew D. Hall, Ann D. Kwong, et al.
Nature Reviews Drug Discovery (2023) Vol. 22, Iss. 7, pp. 585-603
Open Access | Times Cited: 94
Disposition of Nirmatrelvir, an Orally Bioavailable Inhibitor of SARS-CoV-2 3C-Like Protease, across Animals and Humans
Heather Eng, Alyssa Dantonio, Eugene P. Kadar, et al.
Drug Metabolism and Disposition (2022) Vol. 50, Iss. 5, pp. 576-590
Open Access | Times Cited: 89
An orally available Mpro inhibitor is effective against wild-type SARS-CoV-2 and variants including Omicron
Baoxue Quan, Huiping Shuai, Anjie Xia, et al.
Nature Microbiology (2022) Vol. 7, Iss. 5, pp. 716-725
Open Access | Times Cited: 80
Development of optimized drug-like small molecule inhibitors of the SARS-CoV-2 3CL protease for treatment of COVID-19
Hengrui Liu, Sho Iketani, Arie Zask, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 78
Small molecules in the treatment of COVID-19
Sibei Lei, Xiaohua Chen, Jieping Wu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 78
Advances and gaps in SARS-CoV-2 infection models
César Muñoz‐Fontela, Lina Widerspick, Randy A. Albrecht, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 1, pp. e1010161-e1010161
Open Access | Times Cited: 77
Antiviral Drug Discovery for the Treatment of COVID-19 Infections
Teresa I. Ng, Ivan Correia, Jane Seagal, et al.
Viruses (2022) Vol. 14, Iss. 5, pp. 961-961
Open Access | Times Cited: 77
Naturally occurring mutations of SARS-CoV-2 main protease confer drug resistance to nirmatrelvir
Yanmei Hu, Eric M. Lewandowski, Haozhou Tan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 75
S-217622, a SARS-CoV-2 main protease inhibitor, decreases viral load and ameliorates COVID-19 severity in hamsters
Michihito Sasaki, Koshiro Tabata, Mai Kishimoto, et al.
Science Translational Medicine (2022) Vol. 15, Iss. 679
Open Access | Times Cited: 75
Inhibition of the main protease of SARS-CoV-2 (Mpro) by repurposing/designing drug-like substances and utilizing nature’s toolbox of bioactive compounds
Io Antonopoulou, Eleftheria Sapountzaki, Ulrika Rova, et al.
Computational and Structural Biotechnology Journal (2022) Vol. 20, pp. 1306-1344
Open Access | Times Cited: 67
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