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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:

Malleability of the SARS-CoV-2 3CL Mpro Active-Site Cavity Facilitates Binding of Clinical Antivirals
Daniel W. Kneller, Stephanie Galanie, G.N. Phillips, et al.
Structure (2020) Vol. 28, Iss. 12, pp. 1313-1320.e3
Open Access | Times Cited: 123

Showing 1-25 of 123 citing articles:

Structural biology of SARS-CoV-2 and implications for therapeutic development
Haitao Yang, Zihe Rao
Nature Reviews Microbiology (2021) Vol. 19, Iss. 11, pp. 685-700
Open Access | Times Cited: 402
X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
Sebastian Günther, P. Reinke, Yaiza Fernández-García, et al.
Science (2021) Vol. 372, Iss. 6542, pp. 642-646
Open Access | Times Cited: 316
Identification of Inhibitors of SARS-CoV-2 3CL-Pro Enzymatic Activity Using a Small Molecule in Vitro Repurposing Screen
Maria Kuzikov, Elisa Costanzi, Jeanette Reinshagen, et al.
ACS Pharmacology & Translational Science (2021) Vol. 4, Iss. 3, pp. 1096-1110
Open Access | Times Cited: 138
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: 96
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: 67
Structure-based development and preclinical evaluation of the SARS-CoV-2 3C-like protease inhibitor simnotrelvir
Xiangrui Jiang, Haixia Su, Weijuan Shang, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 53
Structure and function of SARS-CoV and SARS-CoV-2 main proteases and their inhibition: A comprehensive review
Xin Li, Yongcheng Song
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115772-115772
Open Access | Times Cited: 51
Rational Design of Hybrid SARS-CoV-2 Main Protease Inhibitors Guided by the Superimposed Cocrystal Structures with the Peptidomimetic Inhibitors GC-376, Telaprevir, and Boceprevir
Zilei Xia, M. Sacco, Yanmei Hu, et al.
ACS Pharmacology & Translational Science (2021) Vol. 4, Iss. 4, pp. 1408-1421
Open Access | Times Cited: 85
High-Throughput Virtual Screening and Validation of a SARS-CoV-2 Main Protease Noncovalent Inhibitor
Austin Clyde, Stephanie Galanie, Daniel W. Kneller, et al.
Journal of Chemical Information and Modeling (2021) Vol. 62, Iss. 1, pp. 116-128
Open Access | Times Cited: 83
In the age of Omicron variant: Paxlovid raises new hopes of COVID‐19 recovery
Zhonglei Wang, Liyan Yang
Journal of Medical Virology (2021) Vol. 94, Iss. 5, pp. 1766-1767
Closed Access | Times Cited: 80
Telaprevir is a potential drug for repurposing against SARS-CoV-2: computational and in vitro studies
Amal Mahmoud, Ahmed Mostafa, Ahmed A. Al‐Karmalawy, et al.
Heliyon (2021) Vol. 7, Iss. 9, pp. e07962-e07962
Open Access | Times Cited: 78
Repurposing the HCV NS3–4A protease drug boceprevir as COVID-19 therapeutics
Rick Oerlemans, Angel J. Ruiz‐Moreno, Yingying Cong, et al.
RSC Medicinal Chemistry (2020) Vol. 12, Iss. 3, pp. 370-379
Open Access | Times Cited: 76
Validation and invalidation of SARS-CoV-2 main protease inhibitors using the Flip-GFP and Protease-Glo luciferase assays
Chunlong Ma, Haozhou Tan, Juliana Choza, et al.
Acta Pharmaceutica Sinica B (2021) Vol. 12, Iss. 4, pp. 1636-1651
Open Access | Times Cited: 72
Hepatitis C virus drugs that inhibit SARS-CoV-2 papain-like protease synergize with remdesivir to suppress viral replication in cell culture
Khushboo Bafna, Kris M. White, Balasubramanian Harish, et al.
Cell Reports (2021) Vol. 35, Iss. 7, pp. 109133-109133
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: 64
SARS-CoV-2 Main Protease Drug Design, Assay Development, and Drug Resistance Studies
Bin Tan, Ryan Joyce, Haozhou Tan, et al.
Accounts of Chemical Research (2022) Vol. 56, Iss. 2, pp. 157-168
Open Access | Times Cited: 61
Design, synthesis and in vitro evaluation of novel SARS-CoV-2 3CLpro covalent inhibitors
Julia Stille, Jevgenijs Tjutrins, Guanyu Wang, et al.
European Journal of Medicinal Chemistry (2021) Vol. 229, pp. 114046-114046
Open Access | Times Cited: 60
SARS-CoV-2 Antiviral Therapy
Kaiming Tao, Philip L. Tzou, Janin Nouhin, et al.
Clinical Microbiology Reviews (2021) Vol. 34, Iss. 4
Open Access | Times Cited: 57
Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor
Nashaat T. Nashed, Annie Aniana, Rodolfo Ghirlando, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 41
SARS-CoV-2 Mpro Inhibitors: Achieved Diversity, Developing Resistance and Future Strategies
Conrad Fischer, Jenson R. Feys
Future Pharmacology (2023) Vol. 3, Iss. 1, pp. 80-107
Open Access | Times Cited: 24
An orally bioavailable SARS-CoV-2 main protease inhibitor exhibits improved affinity and reduced sensitivity to mutations
Michael Westberg, Yichi Su, Xinzhi Zou, et al.
Science Translational Medicine (2024) Vol. 16, Iss. 738
Open Access | Times Cited: 12
MD simulations indicate Omicron P132H of SARS-CoV-2 Mpro is a potential allosteric mutant involved in modulating the dynamics of catalytic site entry loop
Zahoor Ahmad Bhat, Mohd Muzammil Khan, Ayyub Rehman, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130077-130077
Closed Access | Times Cited: 7
Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease
M.G. Deshmukh, Joseph A. Ippolito, Chunhui Zhang, et al.
Structure (2021) Vol. 29, Iss. 8, pp. 823-833.e5
Open Access | Times Cited: 53
Design and Evaluation of Bispidine-Based SARS-CoV-2 Main Protease Inhibitors
Д. Н. Щербаков, Dmitry S. Baev, Mikhail A. Kalinin, et al.
ACS Medicinal Chemistry Letters (2021) Vol. 13, Iss. 1, pp. 140-147
Open Access | Times Cited: 50
Molecular dynamics and in silico mutagenesis on the reversible inhibitor-bound SARS-CoV-2 main protease complexes reveal the role of lateral pocket in enhancing the ligand affinity
Ying Li Weng, Shiv Rakesh Naik, Nadia Dingelstad, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 49
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