Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

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: 70

Showing 1-25 of 70 citing articles:

Roadmap on electronic structure codes in the exascale era
Vikram Gavini, Stefano Baroni, Volker Blüm, et al.
Modelling and Simulation in Materials Science and Engineering (2023) Vol. 31, Iss. 6, pp. 063301-063301
Open Access | Times Cited: 40
In vitro selection of macrocyclic peptide inhibitors containing cyclic γ2,4-amino acids targeting the SARS-CoV-2 main protease
Takashi Miura, Tika R. Malla, David Owen, et al.
Nature Chemistry (2023) Vol. 15, Iss. 7, pp. 998-1005
Open Access | Times Cited: 33
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: 25
The impact of SARS-CoV-2 3CL protease mutations on nirmatrelvir inhibitory efficiency. Computational insights into potential resistance mechanisms
Carlos A. Ramos‐Guzmán, Milorad Andjelkovic, Kirill Zinovjev, et al.
Chemical Science (2023) Vol. 14, Iss. 10, pp. 2686-2697
Open Access | Times Cited: 21
Concordance of X-ray and AlphaFold2 Models of SARS-CoV-2 Main Protease with Residual Dipolar Couplings Measured in Solution
Angus J. Robertson, Joseph M. Courtney, Yang Shen, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 46, pp. 19306-19310
Open Access | Times Cited: 53
Computationally driven discovery of SARS-CoV-2 Mproinhibitors: from design to experimental validation
Léa El Khoury, Zhifeng Jing, Alberto Cuzzolin, et al.
Chemical Science (2022) Vol. 13, Iss. 13, pp. 3674-3687
Open Access | Times Cited: 33
Insights into the binding and covalent inhibition mechanism of PF-07321332 to SARS-CoV-2 Mpro
Son Tung Ngo, Trung Hai Nguyen, Nguyễn Thanh Tùng, et al.
RSC Advances (2022) Vol. 12, Iss. 6, pp. 3729-3737
Open Access | Times Cited: 31
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
Cyclic β2,3-amino acids improve the serum stability of macrocyclic peptide inhibitors targeting the SARS-CoV-2 main protease
Takashi Miura, Tika R. Malla, Lennart Brewitz, et al.
Bulletin of the Chemical Society of Japan (2024) Vol. 97, Iss. 5
Open Access | Times Cited: 6
3-Chymotrypsin-like Protease (3CLpro) of SARS-CoV-2: Validation as a Molecular Target, Proposal of a Novel Catalytic Mechanism, and Inhibitors in Preclinical and Clinical Trials
Vitor Martins de Freitas Amorim, Eduardo Pereira Soares, Anielle Salviano de Almeida Ferrari, et al.
Viruses (2024) Vol. 16, Iss. 6, pp. 844-844
Open Access | Times Cited: 5
Decoding SARS‐CoV‐2 Inhibition: Insights From Molecular Dynamics Simulation of Condensed Amino Thiourea Scaffold Small Molecules
Xiaoli Shen, Hao Zhang, Pengyin Zhang, et al.
Journal of Cellular Biochemistry (2025) Vol. 126, Iss. 2
Closed Access
Dihydropyrimidine-2-thione derivatives as SARS-CoV-2 main protease inhibitors: synthesis, SAR and in vitro profiling
Anees Saeed, Ayesha Tahir, Muhammad Shah, et al.
RSC Advances (2025) Vol. 15, Iss. 8, pp. 6424-6440
Open Access
Determination of SARS-CoV-2 Main Protease (Mpro) Activity Based on Electrooxidation of Tyrosine Residue of a Model Peptide
Tatiana A. Filippova, Rami A. Masamrekh, Tatiana Farafonova, et al.
Biochemistry (Moscow) (2025) Vol. 90, Iss. 1, pp. 120-131
Closed Access
The emerging potential of interactive virtual reality in drug discovery
Rebecca K. Walters, Ella Gale, Jonathan Barnoud, et al.
Expert Opinion on Drug Discovery (2022) Vol. 17, Iss. 7, pp. 685-698
Open Access | Times Cited: 23
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
The S1′–S3′ Pocket of the SARS‐CoV‐2 Main Protease Is Critical for Substrate Selectivity and Can Be Targeted with Covalent Inhibitors
Ming Liu, Jihui Li, Wenqi Liu, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 41
Open Access | Times Cited: 12
Impact of Warhead Modulations on the Covalent Inhibition of SARS-CoV-2 Mpro Explored by QM/MM Simulations
Sérgio Martí, Kemel Arafet, Alessio Lodola, et al.
ACS Catalysis (2021) Vol. 12, Iss. 1, pp. 698-708
Open Access | Times Cited: 27
Ultrafast one-minute electronic detection of SARS-CoV-2 infection by 3CLpro enzymatic activity in untreated saliva samples
Ella Borberg, Eran Granot, Fernando Patolsky
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 21
Computation of Absolute Binding Free Energies for Noncovalent Inhibitors with SARS-CoV-2 Main Protease
Mohammad Mehdi Ghahremanpour, Anastasia Saar, Julian Tirado‐Rives, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 16, pp. 5309-5318
Closed Access | Times Cited: 10
Fullerenes against COVID-19: Repurposing C60 and C70 to Clog the Active Site of SARS-CoV-2 Protease
Tainah Dorina Marforio, Edoardo Jun Mattioli, Francesco Zerbetto, et al.
Molecules (2022) Vol. 27, Iss. 6, pp. 1916-1916
Open Access | Times Cited: 16
Primer for Designing Main Protease (Mpro) Inhibitors of SARS-CoV-2
Abhishek Thakur, Gaurav Sharma, Vishnu Nayak Badavath, et al.
The Journal of Physical Chemistry Letters (2022) Vol. 13, Iss. 25, pp. 5776-5786
Closed Access | Times Cited: 16
Crystal structures of main protease (Mpro) mutants of SARS-CoV-2 variants bound to PF-07304814
Haihai Jiang, Xiaofang Zou, Pei Zeng, et al.
Molecular Biomedicine (2023) Vol. 4, Iss. 1
Open Access | Times Cited: 9
Hydroxamate and thiosemicarbazone: Two highly promising scaffolds for the development of SARS-CoV-2 antivirals
Yin‐Sui Xu, Jia‐Zhu Chigan, Jiaqi Li, et al.
Bioorganic Chemistry (2022) Vol. 124, pp. 105799-105799
Open Access | Times Cited: 14
Computational design of stapled peptide inhibitor against SARS‐CoV‐2 receptor binding domain
Asha Rani Choudhury, Atanu Maity, Sayantani Chakraborty, et al.
Peptide Science (2022) Vol. 114, Iss. 5
Open Access | Times Cited: 14
Upgrading nirmatrelvir to inhibit SARS-CoV-2 Mpro via DeepFrag and free energy calculations
Nguyễn Minh Tâm, Trung Hai Nguyen, Phạm Minh Quân, et al.
Journal of Molecular Graphics and Modelling (2023) Vol. 124, pp. 108535-108535
Open Access | Times Cited: 7
Page 1 - Next Page

Scroll to top