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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:

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

Showing 1-25 of 147 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: 382
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: 208
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
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
SARS-CoV-2 3CL pro mutations selected in a VSV-based system confer resistance to nirmatrelvir, ensitrelvir, and GC376
Emmanuel Heilmann, Francesco Costacurta, Seyed Arad Moghadasi, et al.
Science Translational Medicine (2022) Vol. 15, Iss. 678
Open Access | Times Cited: 103
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
Paxlovid (Nirmatrelvir/Ritonavir): A new approach to Covid-19 therapy?
Seyed Mohammad Reza Hashemian, Amirhossein Sheida, Mohammad Taghizadieh, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 162, pp. 114367-114367
Open Access | Times Cited: 90
Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease
G.D. Noske, Ellen de Souza Silva, Mariana Ortiz de Godoy, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 3, pp. 103004-103004
Open Access | Times Cited: 79
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
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
Nirmatrelvir and risk of hospital admission or death in adults with covid-19: emulation of a randomized target trial using electronic health records
Yan Xie, Benjamin Bowe, Ziyad Al‐Aly
BMJ (2023), pp. e073312-e073312
Open Access | Times Cited: 53
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
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
Genetic Surveillance of SARS-CoV-2 M pro Reveals High Sequence and Structural Conservation Prior to the Introduction of Protease Inhibitor Paxlovid
Jonathan T. Lee, Qingyi Yang, Alexey V. Gribenko, et al.
mBio (2022) Vol. 13, Iss. 4
Open 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
SARS‐CoV‐2 Papain‐Like Protease: Structure, Function and Inhibition
Sven Ullrich, Christoph Nitsche
ChemBioChem (2022) Vol. 23, Iss. 19
Open Access | Times Cited: 43
Ensitrelvir is effective against SARS-CoV-2 3CL protease mutants circulating globally
Sho Kawashima, Yuki Matsui, Takumi Adachi, et al.
Biochemical and Biophysical Research Communications (2023) Vol. 645, pp. 132-136
Open Access | Times Cited: 33
Molecular mechanism of ensitrelvir inhibiting SARS-CoV-2 main protease and its variants
Meng-Meng Lin, Xudong Zeng, Yinkai Duan, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 33
Clinical course and management of COVID-19 in the era of widespread population immunity
Eric A. Meyerowitz, Jake Scott, Aaron Richterman, et al.
Nature Reviews Microbiology (2023) Vol. 22, Iss. 2, pp. 75-88
Closed Access | Times Cited: 33
Nirmatrelvir and COVID-19: development, pharmacokinetics, clinical efficacy, resistance, relapse, and pharmacoeconomics
Daniele Focosi, Scott A. McConnell, Shmuel Shoham, et al.
International Journal of Antimicrobial Agents (2023) Vol. 61, Iss. 2, pp. 106708-106708
Open Access | Times Cited: 31
Antitarget, Anti-SARS-CoV-2 Leads, Drugs, and the Drug Discovery–Genetics Alliance Perspective
Cecilia Pozzi, Anne Vanet, Valeria Francesconi, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 6, pp. 3664-3702
Open Access | Times Cited: 26
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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