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:
The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease
Norman Tran, Sathish Dasari, Sarah Barwell, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 6
Norman Tran, Sathish Dasari, Sarah Barwell, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 6
Showing 6 citing articles:
Revealing the impact of active site residues in modeling the inhibition mechanism of SARS-Cov-2 main protease by GC373
Mohamed M. Aboelnga, Maya Petgrave, Subha Kalyaanamoorthy, et al.
Computers in Biology and Medicine (2025) Vol. 187, pp. 109779-109779
Closed Access
Mohamed M. Aboelnga, Maya Petgrave, Subha Kalyaanamoorthy, et al.
Computers in Biology and Medicine (2025) Vol. 187, pp. 109779-109779
Closed Access
SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds
P. Reinke, Robin Schubert, Dominik Oberthür, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
P. Reinke, Robin Schubert, Dominik Oberthür, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Mechanistic Insights into the Mutational Landscape of the Main Protease/3CLPro and Its Impact on Long-Term COVID-19/SARS-CoV-2 Management
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonjabulo Ntombikhona Magwaza, et al.
(2024)
Open Access | Times Cited: 1
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonjabulo Ntombikhona Magwaza, et al.
(2024)
Open Access | Times Cited: 1
The Conformational Space of the SARS-CoV-2 Main Protease Active Site Loops Is Determined by Ligand Binding and Interprotomer Allostery
Ethan Lee, Sarah Rauscher
Biochemistry (2024) Vol. 64, Iss. 1, pp. 32-46
Open Access
Ethan Lee, Sarah Rauscher
Biochemistry (2024) Vol. 64, Iss. 1, pp. 32-46
Open Access
SARS-CoV-2 main protease (M-pro) mutational profiling: An insight into mutation coldspots
Pol Garcia‐Segura, Ariadna Llop-Peiró, Nil Novau-Ferré, et al.
Computers in Biology and Medicine (2024) Vol. 184, pp. 109344-109344
Open Access
Pol Garcia‐Segura, Ariadna Llop-Peiró, Nil Novau-Ferré, et al.
Computers in Biology and Medicine (2024) Vol. 184, pp. 109344-109344
Open Access
Mechanistic Insights into the Mutational Landscape of the Main Protease/3CLPro and Its Impact on Long-Term COVID-19/SARS-CoV-2 Management
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonjabulo Ntombikhona Magwaza, et al.
Future Pharmacology (2024) Vol. 4, Iss. 4, pp. 825-852
Open Access
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonjabulo Ntombikhona Magwaza, et al.
Future Pharmacology (2024) Vol. 4, Iss. 4, pp. 825-852
Open Access
The Conformational Space of the SARS-CoV-2 Main Protease Active Site Loops is Determined by Ligand Binding and Interprotomer Allostery
Ethan Lee, Sarah Rauscher
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Ethan Lee, Sarah Rauscher
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
