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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:

A yeast-based system to study SARS-CoV-2 Mpro structure and to identify nirmatrelvir resistant mutations
Jin Ou, Eric M. Lewandowski, Yanmei Hu, et al.
PLoS Pathogens (2023) Vol. 19, Iss. 8, pp. e1011592-e1011592
Open Access | Times Cited: 21

Showing 21 citing articles:

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
Systematic Analyses of the Resistance Potential of Drugs Targeting SARS-CoV-2 Main Protease
Julia M. Flynn, Qiu Yu J. Huang, Sarah N. Zvornicanin, et al.
ACS Infectious Diseases (2023) Vol. 9, Iss. 7, pp. 1372-1386
Open Access | Times Cited: 23
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
Structural Basis for Coronaviral Main Proteases Inhibition by the 3CLpro Inhibitor GC376
Cheng‐Wen Lin, Zhu Zhi-min, Haihai Jiang, et al.
Journal of Molecular Biology (2024) Vol. 436, Iss. 6, pp. 168474-168474
Closed Access | Times Cited: 8
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: 7
Hotspot residues and resistance mutations in the nirmatrelvir-binding site of SARS-CoV-2 main protease: Design, identification, and correlation with globally circulating viral genomes
Aditya K. Padhi, Timir Tripathi
Biochemical and Biophysical Research Communications (2022) Vol. 629, pp. 54-60
Open Access | Times Cited: 35
Unveiling the mechanism of action of a novel natural dual inhibitor of SARS-CoV-2 Mpro and PLpro with molecular dynamics simulations
Xiaoxia Gu, Xiaotian Zhang, Xueke Zhang, et al.
Natural Products and Bioprospecting (2025) Vol. 15, Iss. 1
Open Access
Exploring Possible Drug-Resistant Variants of SARS-CoV-2 Main Protease (Mpro) with Noncovalent Preclinical Candidate, Mpro61
Jessica R. Kenneson, Christina Papini, Su Tang, et al.
ACS Bio & Med Chem Au (2025)
Open Access
Potent antiviral activity of simnotrelvir against key epidemic SARS-CoV-2 variants with a high resistance barrier
Liwei Zhao, Chuang Li, Mengyu Wang, et al.
Antimicrobial Agents and Chemotherapy (2025)
Open Access
Exploring the structural and molecular interaction landscape of nirmatrelvir and Mpro complex: The study might assist in designing more potent antivirals targeting SARS-CoV-2 and other viruses
Chiranjib Chakraborty, Manojit Bhattacharya, Abdulrahman Alshammari, et al.
Journal of Infection and Public Health (2023) Vol. 16, Iss. 12, pp. 1961-1970
Open Access | Times Cited: 12
A comprehensive study of SARS-CoV-2 main protease (Mpro) inhibitor-resistant mutants selected in a VSV-based system
Francesco Costacurta, Andrea Dodaro, David Bante, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 8
Dopamine and its precursor levodopa inactivate SARS-CoV-2 main protease by forming a quinoprotein
Meng Hao, Yufeng He, Tingting Song, et al.
Free Radical Biology and Medicine (2024) Vol. 220, pp. 167-178
Closed Access | Times Cited: 2
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: 2
A community effort in SARS‐CoV‐2 drug discovery
Johannes Schimunek, Philipp Seidl, Katarina Elez, et al.
Molecular Informatics (2023) Vol. 43, Iss. 1
Open Access | Times Cited: 7
Sierra SARS-CoV-2 sequence and antiviral resistance analysis program
Philip L. Tzou, Kaiming Tao, Malaya K. Sahoo, et al.
Journal of Clinical Virology (2022) Vol. 157, pp. 105323-105323
Open Access | Times Cited: 10
A comprehensive study of SARS-CoV-2 mfigain protease (Mpro) inhibitor-resistant mutants selected in a VSV-based system
Francesco Costacurta, Andrea Dodaro, David Bante, et al.
PLoS Pathogens (2024) Vol. 20, Iss. 9, pp. e1012522-e1012522
Open Access | Times Cited: 1
An automated positive selection screen in yeast provides support for boron-containing compounds as inhibitors of SARS-CoV-2 main protease
Sunniva Sigurdardóttir, Suélen Fernandes Silva, Ievgeniia Tiukova, et al.
Microbiology Spectrum (2024) Vol. 12, Iss. 10
Open Access
An Investigation of Nirmatrelvir (Paxlovid) Resistance in SARS-CoV-2 Mpro
Rasha M. Yaghi, Dennis Wylie, Collin L. Andrews, et al.
ACS Bio & Med Chem Au (2024) Vol. 4, Iss. 6, pp. 280-290
Open Access
SARS-CoV-2 main protease (M-pro) mutational profiling: An insight into mutation coldspots
Pol Garcia‐Segura, Ariadna Llop-Peiró, Nil Novau-Ferré, et al.
Computers in Biology and Medicine (2024) Vol. 184, pp. 109344-109344
Open Access
Backstage Heroes—Yeast in COVID-19 Research
Wojciech Grabiński, Andonis Karachitos, Anna Kicińska
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 23, pp. 12661-12661
Open Access
Meisoindigo: An Effective Inhibitor of SARS-CoV-2 Main Protease Revealed by Yeast System
Wojciech Grabiński, Anna Kicińska, Ewa Kosicka, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
No emergence of resistance mutations in COVID‐19 patients receiving nirmatrelvir/ritonavir
Rosalía Palomino‐Cabrera, Francisco Tejerina, Andrea Molero‐Salinas, et al.
Journal of Medical Virology (2023) Vol. 96, Iss. 1
Closed Access | Times Cited: 1
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