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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:

Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease
Elizabeth A. MacDonald, Gary Frey, Mark Namchuk, et al.
ACS Infectious Diseases (2021) Vol. 7, Iss. 9, pp. 2591-2595
Open Access | Times Cited: 73

Showing 1-25 of 73 citing articles:

Nirmatrelvir-resistant SARS-CoV-2 variants with high fitness in an infectious cell culture system
Yuyong Zhou, Karen Anbro Gammeltoft, Line A. Ryberg, et al.
Science Advances (2022) Vol. 8, Iss. 51
Open Access | Times Cited: 175
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease
Daniel W. Kneller, Hui Li, G.N. Phillips, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 100
Defining the substrate envelope of SARS-CoV-2 main protease to predict and avoid drug resistance
Ala M. Shaqra, Sarah N. Zvornicanin, Qiu Yu J. Huang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 99
Comprehensive fitness landscape of SARS-CoV-2 Mpro reveals insights into viral resistance mechanisms
Julia M. Flynn, Neha S. Samant, Gily Schneider-Nachum, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 98
Inhibition of the main protease of SARS-CoV-2 (Mpro) by repurposing/designing drug-like substances and utilizing nature’s toolbox of bioactive compounds
Io Antonopoulou, Eleftheria Sapountzaki, Ulrika Rova, et al.
Computational and Structural Biotechnology Journal (2022) Vol. 20, pp. 1306-1344
Open Access | Times Cited: 70
X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation
Jaeyong Lee, Calem Kenward, L.J. Worrall, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 67
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: 63
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
Dynamical Nonequilibrium Molecular Dynamics Simulations Identify Allosteric Sites and Positions Associated with Drug Resistance in the SARS-CoV-2 Main Protease
H. T. Henry Chan, A. Sofia F. Oliveira, Christopher J. Schofield, et al.
JACS Au (2023) Vol. 3, Iss. 6, pp. 1767-1774
Open Access | Times Cited: 30
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
Invention of MK-7845, a SARS-CoV-2 3CL Protease Inhibitor Employing a Novel Difluorinated Glutamine Mimic
Valerie W. Shurtleff, M. E. Layton, Craig A. Parish, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 5, pp. 3935-3958
Closed Access | Times Cited: 12
Inhibitors of SARS-CoV-2 Main Protease (Mpro) as Anti-Coronavirus Agents
Agnieszka Zagórska, Anna Czopek, Monika Fryc, et al.
Biomolecules (2024) Vol. 14, Iss. 7, pp. 797-797
Open Access | Times Cited: 10
The NSP4 T492I mutation increases SARS-CoV-2 infectivity by altering non-structural protein cleavage
Xiaoyuan Lin, Zhou Sha, Jakob Trimpert, et al.
Cell Host & Microbe (2023) Vol. 31, Iss. 7, pp. 1170-1184.e7
Open Access | Times Cited: 19
SARS-CoV-2 polyprotein substrate regulates the stepwise Mpro cleavage reaction
M. Narwal, Jean‐Paul Armache, Thomas J. Edwards, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 5, pp. 104697-104697
Open Access | Times Cited: 18
Contribution of the catalytic dyad of SARS-CoV-2 main protease to binding covalent and noncovalent inhibitors
Andrey Kovalevsky, Annie Aniana, Leighton Coates, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 7, pp. 104886-104886
Open Access | Times Cited: 18
Advances in the discovery of new chemotypes through ultra-large library docking
Felix Potlitz, Andreas Link, Lukas Schulig
Expert Opinion on Drug Discovery (2023) Vol. 18, Iss. 3, pp. 303-313
Closed Access | Times Cited: 17
MDM-TASK-web: MD-TASK and MODE-TASK web server for analyzing protein dynamics
Olivier Sheik Amamuddy, Michael Glenister, Thulani Tshabalala, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 5059-5071
Open Access | Times Cited: 37
Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursors
Annie Aniana, Nashaat T. Nashed, Rodolfo Ghirlando, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 16
AI-Accelerated Design of Targeted Covalent Inhibitors for SARS-CoV-2
Rajendra P. Joshi, Katherine Schultz, Jesse Wilson, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 5, pp. 1438-1453
Open Access | Times Cited: 14
Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket
Chia‐Ying Huang, A. Metz, Roland Lange, et al.
Acta Crystallographica Section D Structural Biology (2024) Vol. 80, Iss. 2, pp. 123-136
Open Access | Times Cited: 6
A Comprehensive Update of Anti-COVID-19 Activity of Heterocyclic Compounds
M. Tariq Nazir, Matloob Ahmad, Sana Aslam, et al.
Drug Design Development and Therapy (2024) Vol. Volume 18, pp. 1547-1571
Open Access | Times Cited: 6
Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 Main Protease using a linked protein FRET platform
Calem Kenward, M. Vuckovic, Mark Paetzel, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107367-107367
Open Access | Times Cited: 6
Computational evaluation and benchmark study of 342 crystallographic holo-structures of SARS-CoV-2 Mpro enzyme
Hamlet Khachatryan, Mher Matevosyan, Vardan Harutyunyan, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 6
Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro
Ruchi Yadav, Valentine V. Courouble, Sanjay Kumar Dey, et al.
Science Advances (2022) Vol. 8, Iss. 49
Open Access | Times Cited: 21
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: 13
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