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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:

Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
Jaeyong Lee, L.J. Worrall, M. Vuckovic, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 212

Showing 1-25 of 212 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
Structural basis for replicase polyprotein cleavage and substrate specificity of main protease from SARS-CoV-2
Yao Zhao, Yan Zhu, Xiang Liu, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 16
Open Access | Times Cited: 130
Catalytic Dyad Residues His41 and Cys145 Impact the Catalytic Activity and Overall Conformational Fold of the Main SARS-CoV-2 Protease 3-Chymotrypsin-Like Protease
Juliana C. Ferreira, Samar Fadl, Adrian J. Villanueva, et al.
Frontiers in Chemistry (2021) Vol. 9
Open Access | Times Cited: 110
Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease
G.D. Noske, Ellen de Souza Silva, Mariana Ortiz de Godoy, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 3, pp. 103004-103004
Open Access | Times Cited: 83
SARS-CoV-2 and the Host Cell: A Tale of Interactions
Massimo Pizzato, Chiara Baraldi, Giulia Boscato Sopetto, et al.
Frontiers in Virology (2022) Vol. 1
Open Access | Times Cited: 72
SARS-CoV-2 Mpro Protease Variants of Concern Display Altered Viral Substrate and Cell Host Target Galectin-8 Processing but Retain Sensitivity toward Antivirals
Sizhu Amelia Chen, Elena Arutyunova, Jimmy Lu, et al.
ACS Central Science (2023) Vol. 9, Iss. 4, pp. 696-708
Open Access | Times Cited: 46
Perspectives on SARS-CoV-2 Main Protease Inhibitors
Kaifu Gao, Rui Wang, Jiahui Chen, et al.
Journal of Medicinal Chemistry (2021) Vol. 64, Iss. 23, pp. 16922-16955
Open Access | Times Cited: 94
Mechanistic insights into COVID-19 by global analysis of the SARS-CoV-2 3CLpro substrate degradome
Isabel Pablos, Yoan Machado, Hugo César Ramos de Jesus, et al.
Cell Reports (2021) Vol. 37, Iss. 4, pp. 109892-109892
Open Access | Times Cited: 87
Discovery of SARS-CoV-2 Mpro peptide inhibitors from modelling substrate and ligand binding
H. T. Henry Chan, Marc A. Moesser, Rebecca K. Walters, et al.
Chemical Science (2021) Vol. 12, Iss. 41, pp. 13686-13703
Open Access | Times Cited: 74
The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors
Lucia Silvestrini, Norhan Belhaj, Lucia Comez, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 73
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
Investigating the structure–activity relationship of marine natural polyketides as promising SARS-CoV-2 main protease inhibitors
Amr El‐Demerdash, Ahmed A. Al‐Karmalawy, Tarek Mohamed Abd El‐Aziz, et al.
RSC Advances (2021) Vol. 11, Iss. 50, pp. 31339-31363
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
A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process
G.D. Noske, A.M. Nakamura, Victor O. Gawriljuk, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 18, pp. 167118-167118
Open Access | Times Cited: 66
Viral proteases: Structure, mechanism and inhibition
Jacqueto Zephyr, Neşe Kurt Yılmaz, Celia A. Schiffer
˜The œEnzymes (2021), pp. 301-333
Open Access | Times Cited: 65
A structural view of the SARS-CoV-2 virus and its assembly
Nathan Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
SARS-CoV-2 main protease suppresses type I interferon production by preventing nuclear translocation of phosphorylated IRF3
Sin‐Yee Fung, Kam‐Leung Siu, Huayue Lin, et al.
International Journal of Biological Sciences (2021) Vol. 17, Iss. 6, pp. 1547-1554
Open Access | Times Cited: 62
Automated discovery of noncovalent inhibitors of SARS-CoV-2 main protease by consensus Deep Docking of 40 billion small molecules
Francesco Gentile, Michael Fernández, Fuqiang Ban, et al.
Chemical Science (2021) Vol. 12, Iss. 48, pp. 15960-15974
Open Access | Times Cited: 57
Antiviral cyclic peptides targeting the main protease of SARS-CoV-2
Jason Johansen‐Leete, Sven Ullrich, Sarah E. Fry, et al.
Chemical Science (2022) Vol. 13, Iss. 13, pp. 3826-3836
Open Access | Times Cited: 50
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
Key dimer interface residues impact the catalytic activity of 3CLpro, the main protease of SARS-CoV-2
Juliana C. Ferreira, Samar Fadl, Wael M. Rabeh
Journal of Biological Chemistry (2022) Vol. 298, Iss. 6, pp. 102023-102023
Open Access | Times Cited: 44
The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro)
Ali Ebrahim, Blake T. Riley, D. Kumaran, et al.
IUCrJ (2022) Vol. 9, Iss. 5, pp. 682-694
Open Access | Times Cited: 44
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
Structural biology of SARS-CoV-2 Mpro and drug discovery
Yinkai Duan, Haofeng Wang, Zhenghong Yuan, et al.
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102667-102667
Closed Access | Times Cited: 24
Multiple redox switches of the SARS-CoV-2 main protease in vitro provide opportunities for drug design
Lisa-Marie Funk, Gereon Poschmann, Fabian Rabe von Pappenheim, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
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