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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 Variants with High Fitness in Vitro
Yuyong Zhou, Karen Anbro Gammeltoft, Line A. Ryberg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Multiple pathways for SARS-CoV-2 resistance to nirmatrelvir
Sho Iketani, Hiroshi Mohri, Bruce Culbertson, et al.
Nature (2022) Vol. 613, Iss. 7944, pp. 558-564
Open Access | Times Cited: 329
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: 134
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: 85
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
Sequential intrahost evolution and onward transmission of SARS-CoV-2 variants
Ana S. González-Reiche, Hala Alshammary, Sarah Schaefer, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 66
Functional map of SARS-CoV-2 3CL protease reveals tolerant and immutable sites
Sho Iketani, Seo Jung Hong, Jenny Sheng, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 10, pp. 1354-1362.e6
Open Access | Times Cited: 50
Multiple pathways for SARS-CoV-2 resistance to nirmatrelvir
Sho Iketani, Hiroshi Mohri, Bruce Culbertson, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 44
The substitutions L50F, E166A and L167F in SARS-CoV-2 3CLpro are selected by a protease inhibitorin vitroand confer resistance to nirmatrelvir
Dirk Jochmans, Liu C, Kim Donckers, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 42
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: 32
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: 25
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: 37
Combinations of Host- and Virus-Targeting Antiviral Drugs Confer Synergistic Suppression of SARS-CoV-2
Jessica Wagoner, Shawn Herring, Tien-Ying Hsiang, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 5
Open Access | Times Cited: 37
Predicting Antiviral Resistance Mutations in SARS-CoV-2 Main Protease with Computational and Experimental Screening
Vishnu Mini Sasi, Sven Ullrich, Jennifer Ton, et al.
Biochemistry (2022) Vol. 61, Iss. 22, pp. 2495-2505
Open Access | Times Cited: 36
Viral proteases as therapeutic targets
Taťána Majerová, Jan Konvalinka
Molecular Aspects of Medicine (2022) Vol. 88, pp. 101159-101159
Open Access | Times Cited: 35
Combined molnupiravir-nirmatrelvir treatment improves the inhibitory effect on SARS-CoV-2 in macaques
Kyle Rosenke, Matt C. Lewis, Friederike Feldmann, et al.
JCI Insight (2022) Vol. 8, Iss. 4
Open Access | Times Cited: 32
Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors
Seyed Arad Moghadasi, Emmanuel Heilmann, Ahmed Magdy Khalil, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 31
A retrospective cohort study of Paxlovid efficacy depending on treatment time in hospitalized COVID-19 patients
Zhanwei Du, Lin Wang, Yuan Bai, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 7
The Antiviral Effects of 2-Deoxy-D-glucose (2-DG), a Dual D-Glucose and D-Mannose Mimetic, against SARS-CoV-2 and Other Highly Pathogenic Viruses
Beata Pająk, Rafał Zieliński, John T. Manning, et al.
Molecules (2022) Vol. 27, Iss. 18, pp. 5928-5928
Open Access | Times Cited: 25
A proof-of-concept study on the genomic evolution of Sars-Cov-2 in molnupiravir-treated, paxlovid-treated and drug-naïve patients
Claudia Alteri, Valeria Fox, Rossana Scutari, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 23
A guide to COVID‐19 antiviral therapeutics: a summary and perspective of the antiviral weapons against SARS‐CoV‐2 infection
Drugan K. Brady, Aashi R. Gurijala, Liyu Huang, et al.
FEBS Journal (2022) Vol. 291, Iss. 8, pp. 1632-1662
Open Access | Times Cited: 21
Optimized ACE2 decoys neutralize antibody-resistant SARS-CoV-2 variants through functional receptor mimicry and treat infection in vivo
James A. Torchia, Alexander H. Tavares, Laura Stentoft Carstensen, et al.
Science Advances (2022) Vol. 8, Iss. 49
Open Access | Times Cited: 20
Computational design of nanomolar-binding antibodies specific to multiple SARS-CoV-2 variants by engineering a specificity switch of antibody 80R using RosettaAntibodyDesign (RAbD) results in potential generalizable therapeutic antibodies for novel SARS-CoV-2 virus
Nancy Hernandez, Wojciech Jankowski, Rahel Frick, et al.
Heliyon (2023) Vol. 9, Iss. 4, pp. e15032-e15032
Open Access | Times Cited: 10
Polyphenolic promiscuity, inflammation-coupled selectivity: Whether PAINs filters mask an antiviral asset
Rick Sheridan, Kevin Spelman
Frontiers in Pharmacology (2022) Vol. 13
Open Access | Times Cited: 13
SARS-CoV-2 variants in the making: Sequential intrahost evolution and forward transmissions in the context of persistent infections
Ana S. González-Reiche, Hala Alshammary, Sarah Schaefer, et al.
medRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 12
Recent changes in the mutational dynamics of the SARS-CoV-2 main protease substantiate the danger of emerging resistance to antiviral drugs
Lena Parigger, A. Krassnigg, Tobias Schopper, et al.
Frontiers in Medicine (2022) Vol. 9
Open Access | Times Cited: 12
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