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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:

The mechanism of RNA capping by SARS-CoV-2
Gina J. Park, Adam Osinski, Genaro Hernandez, et al.
Nature (2022)
Open Access | Times Cited: 90

Showing 1-25 of 90 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: 420
SARS-CoV-2 biology and host interactions
Silvio Steiner, Annika Kratzel, G. Tuba Barut, et al.
Nature Reviews Microbiology (2024) Vol. 22, Iss. 4, pp. 206-225
Closed Access | Times Cited: 81
Structural basis for substrate selection by the SARS-CoV-2 replicase
Brandon Malone, Jason K. Perry, Paul Dominic B. Olinares, et al.
Nature (2023) Vol. 614, Iss. 7949, pp. 781-787
Open Access | Times Cited: 47
Metabolic alterations upon SARS-CoV-2 infection and potential therapeutic targets against coronavirus infection
Peiran Chen, Mandi Wu, Yaqing He, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 34
Classification of domains in predicted structures of the human proteome
R. Dustin Schaeffer, Jing Zhang, Lisa N. Kinch, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 12
Open Access | Times Cited: 29
SND1 binds SARS-CoV-2 negative-sense RNA and promotes viral RNA synthesis through NSP9
Nora Schmidt, Sabina Ganskih, Yuanjie Wei, et al.
Cell (2023) Vol. 186, Iss. 22, pp. 4834-4850.e23
Open Access | Times Cited: 29
A mechanism for SARS-CoV-2 RNA capping and its inhibition by nucleotide analog inhibitors
Liming Yan, Yucen Huang, Ji Ge, et al.
Cell (2022) Vol. 185, Iss. 23, pp. 4347-4360.e17
Open Access | Times Cited: 37
Viral evasion of the interferon response at a glance
Junji Zhu, Cindy Chiang, Michaela U. Gack
Journal of Cell Science (2023) Vol. 136, Iss. 12
Open Access | Times Cited: 21
Coronavirus takeover of host cell translation and intracellular antiviral response: a molecular perspective
Evangelos D. Karousis, Katharina Schubert, Nenad Ban
The EMBO Journal (2024) Vol. 43, Iss. 2, pp. 151-167
Open Access | Times Cited: 8
Despite the odds: formation of the SARS-CoV-2 methylation complex
Alex Matsuda, Jacek Plewka, Michał Rawski, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 11, pp. 6441-6458
Open Access | Times Cited: 7
Nanoscale cellular organization of viral RNA and proteins in SARS-CoV-2 replication organelles
Leonid Andronov, Mengting Han, Yan‐Yu Zhu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Progress in Research on Inhibitors Targeting SARS-CoV-2 Main Protease (Mpro)
Yue Yang, Yidan Luo, Chenbo Zhang, et al.
ACS Omega (2024) Vol. 9, Iss. 32, pp. 34196-34219
Open Access | Times Cited: 6
Looking lively: emerging principles of pseudokinase signaling
Joshua B. Sheetz, Mark A. Lemmon
Trends in Biochemical Sciences (2022) Vol. 47, Iss. 10, pp. 875-891
Open Access | Times Cited: 27
Kill or corrupt: Mechanisms of action and drug-resistance of nucleotide analogues against SARS-CoV-2
Ashleigh Shannon, Bruno Canard
Antiviral Research (2022) Vol. 210, pp. 105501-105501
Open Access | Times Cited: 25
A universal fluorescence polarization high throughput screening assay to target the SAM-binding sites of SARS-CoV-2 and other viral methyltransferases
Subodh Kumar Samrat, Qamar Bashir, Ran Zhang, et al.
Emerging Microbes & Infections (2023) Vol. 12, Iss. 1
Open Access | Times Cited: 14
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
Filip Mihalič, Caroline Benz, Eszter Kassa, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13
Tonsils are major sites of persistence of SARS-CoV-2 in children
Thais M. Lima, Ronaldo B. Martins, Carolina Sponchiado Miura, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 5
Open Access | Times Cited: 13
Rational Design of Highly Potent SARS-CoV-2 nsp14 Methyltransferase Inhibitors
Milan Štefek, Dominika Chalupská, Karel Chalupský, et al.
ACS Omega (2023) Vol. 8, Iss. 30, pp. 27410-27418
Open Access | Times Cited: 11
Small-molecule inhibition of SARS-CoV-2 NSP14 RNA cap methyltransferase
Cindy Meyer, Aitor Garzia, Michael W. Miller, et al.
Nature (2024)
Closed Access | Times Cited: 4
Transcription Kinetics in the Coronavirus Life Cycle
Katarzyna Grelewska‐Nowotko, Ahmed Eısa Elhag, Tomasz W. Turowski
Wiley Interdisciplinary Reviews - RNA (2025) Vol. 16, Iss. 1
Open Access
Anti-interferon armamentarium of human coronaviruses
Oyahida Khatun, Sumandeep Kaur, Shashank Tripathi
Cellular and Molecular Life Sciences (2025) Vol. 82, Iss. 1
Open Access
Contribution to pathogenesis of accessory proteins of deadly human coronaviruses
Jesús Hurtado-Tamayo, Ricardo Requena-Platek, Luis Enjuanes, et al.
Frontiers in Cellular and Infection Microbiology (2023) Vol. 13
Open Access | Times Cited: 10
Nsp14 of SARS-CoV-2 inhibits mRNA processing and nuclear export by targeting the nuclear cap-binding complex
Jun Katahira, Tatsuya Ohmae, Mayo Yasugi, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 14, pp. 7602-7618
Open Access | Times Cited: 10
Emerging variants of SARS-CoV-2 NSP10 highlight strong functional conservation of its binding to two non-structural proteins, NSP14 and NSP16
Huan Wang, Syed RA Rizvi, Danni Dong, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 10
Discovery of a Druggable, Cryptic Pocket in SARS-CoV-2 nsp16 Using Allosteric Inhibitors
Nicole L. Inniss, Ján Kozic, Fengling Li, et al.
ACS Infectious Diseases (2023) Vol. 9, Iss. 10, pp. 1918-1931
Open Access | Times Cited: 10
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