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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:

Nirmatrelvir-resistant SARS-CoV-2 is efficiently transmitted in female Syrian hamsters and retains partial susceptibility to treatment
Rana Abdelnabi, Dirk Jochmans, Kim Donckers, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20

Showing 20 citing articles:

Global prevalence of SARS-CoV-2 3CL protease mutations associated with nirmatrelvir or ensitrelvir resistance
Jonathan Daniel Ip, Allen Wing‐Ho Chu, Wan-Mui Chan, et al.
EBioMedicine (2023) Vol. 91, pp. 104559-104559
Open Access | Times Cited: 69
Nirmatrelvir Resistance—de Novo E166V/L50V Mutations in an Immunocompromised Patient Treated With Prolonged Nirmatrelvir/Ritonavir Monotherapy Leading to Clinical and Virological Treatment Failure—a Case Report
Neta S. Zuckerman, Efrat Bucris, Danielle Keidar-Friedman, et al.
Clinical Infectious Diseases (2023) Vol. 78, Iss. 2, pp. 352-355
Closed Access | Times Cited: 53
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
In vitro and in vivo characterization of SARS-CoV-2 strains resistant to nirmatrelvir
Maki Kiso, Yuri Furusawa, Ryuta Uraki, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
An orally bioavailable SARS-CoV-2 main protease inhibitor exhibits improved affinity and reduced sensitivity to mutations
Michael Westberg, Yichi Su, Xinzhi Zou, et al.
Science Translational Medicine (2024) Vol. 16, Iss. 738
Open Access | Times Cited: 12
Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04
Lijing Zhang, Xuping Xie, Hannan Luo, et al.
Cell Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 11
SARS-CoV-2 resistance to monoclonal antibodies and small-molecule drugs
Sho Iketani, David D. Ho
Cell chemical biology (2024) Vol. 31, Iss. 4, pp. 632-657
Open Access | Times Cited: 8
Design, Synthesis, and Unprecedented Interactions of Covalent Dipeptide-Based Inhibitors of SARS-CoV-2 Main Protease and Its Variants Displaying Potent Antiviral Activity
Philipp Flury, Nadine Krüger, Katharina Sylvester, et al.
Journal of Medicinal Chemistry (2025)
Closed Access
Substitutions in SARS-CoV-2 Mpro Selected by Protease Inhibitor Boceprevir Confer Resistance to Nirmatrelvir
Karen Anbro Gammeltoft, Yuyong Zhou, Line A. Ryberg, et al.
Viruses (2023) Vol. 15, Iss. 9, pp. 1970-1970
Open Access | Times Cited: 12
Distal protein-protein interactions contribute to nirmatrelvir resistance
Eric M. Lewandowski, Xiujun Zhang, Haozhou Tan, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Design of quinoline SARS-CoV-2 papain-like protease inhibitors as oral antiviral drug candidates
Prakash D. Jadhav, Xueying Liang, Ahmadullah Ansari, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
A coronavirus assembly inhibitor that targets the viral membrane protein
Manon Laporte, Dirk Jochmans, Dorothée Bardiot, et al.
Nature (2025)
Open Access
Highly specific SARS-CoV-2 main protease (Mpro) mutations against the clinical antiviral ensitrelvir selected in a safe, VSV-based system
Stefanie Rauch, Francesco Costacurta, Helge Schöppe, et al.
Antiviral Research (2024) Vol. 231, pp. 105969-105969
Open Access | Times Cited: 3
Distal Protein-Protein Interactions Contribute to SARS-CoV-2 Main Protease Substrate Binding and Nirmatrelvir Resistance
Eric M. Lewandowski, Xiujun Zhang, Haozhou Tan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
The importance of good practices and false hits for QSAR-driven virtual screening real application: a SARS-CoV-2 main protease (Mpro) case study
Mateus Sá Magalhães Serafim, Simone Queiroz Pantaleão, Elany Barbosa da Silva, et al.
Frontiers in Drug Discovery (2023) Vol. 3
Open Access | Times Cited: 6
Identification of a novel inhibitor of SARS‐CoV‐2 main protease: an in silico, biochemical, and cell‐based approach
Aditya Trivedi, Vandana Kardam, Krishna Kishore Inampudi, et al.
FEBS Journal (2023) Vol. 290, Iss. 23, pp. 5496-5513
Closed Access | Times Cited: 4
New anti-SARS-CoV-2 aminoadamantane compounds as antiviral candidates for the treatment of COVID-19
Daisymara Priscila de Almeida Marques, Luis Adan Flores Andrade, Erik Vinicius Sousa Reis, et al.
Virus Research (2023) Vol. 340, pp. 199291-199291
Open Access | Times Cited: 2
Drug Susceptibility and the Potential for Drug-Resistant SARS-CoV-2 Emergence in Immunocompromised Animals
Maki Kiso, Ryuta Uraki, Seiya Yamayoshi, et al.
iScience (2024) Vol. 27, Iss. 9, pp. 110729-110729
Open Access
Characterization of a SARS-CoV-2 Omicron BA.5 direct-contact transmission model in hamsters
Kim Handrejk, Katharina S. Schmitz, Edwin J. B. Veldhuis Kroeze, et al.
npj Viruses (2024) Vol. 2, Iss. 1
Open Access
Design of SARS-CoV-2 protease inhibitors with improved affinity and reduced sensitivity to mutations
Michael Westberg, Yichi Su, Xinzhi Zou, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04
Lijing Zhang, Xuping Xie, Hannan Luo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
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