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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:

Unraveling the catalytic mechanism of SARS-CoV-2 papain-like protease with allosteric modulation of C270 mutation using multiscale computational approaches
Qiang Shao, Muya Xiong, Jiameng Li, et al.
Chemical Science (2023) Vol. 14, Iss. 18, pp. 4681-4696
Open Access | Times Cited: 13

Showing 13 citing articles:

Identification Mechanism of BACE1 on Inhibitors Probed by Using Multiple Separate Molecular Dynamics Simulations and Comparative Calculations of Binding Free Energies
Yiwen Wang, Fen Yang, Dongliang Yan, et al.
Molecules (2023) Vol. 28, Iss. 12, pp. 4773-4773
Open Access | Times Cited: 14
Mutational profiling of SARS-CoV-2 papain-like protease reveals requirements for function, structure, and drug escape
Xinyu Wu, Margareta Go, Julie V. Nguyen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Pyrylium derivatives as outer membrane permeabilizers against MDR Gram-negative bacteria via multi-target mode of action
Qionglu Duan, Min Yuan, Xican Ma, et al.
European Journal of Medicinal Chemistry (2025) Vol. 289, pp. 117387-117387
Closed Access
Dynamic Cap‐Mediated Substrate Access and Potent Inhibitor Design of Monkeypox Virus I7L Protease
Haixia Su, Guoqing Wu, Muya Xiong, et al.
Advanced Science (2025)
Open Access
Analysis of Structures of SARS-CoV-2 Papain-like Protease Bound with Ligands Unveils Structural Features for Inhibiting the Enzyme
Ann Varghese, Jie Liu, Bailang Liu, et al.
Molecules (2025) Vol. 30, Iss. 3, pp. 491-491
Open Access
Identification Mechanism of BACE1 on Inhibitors Probed by Using Multiple Separate Molecular Dynamics Simulations and Comparative Calculations of Binding Free Energies
Y. Wang, Fen Yang, Dongliang Yan, et al.
(2023)
Open Access | Times Cited: 6
Covalent DNA-Encoded Library Workflow Drives Discovery of SARS-CoV-2 Non-structural Proteins Inhibitors
Xiaojie Lu, Hangchen Hu, Lianghe Mei, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Native Mass Spectrometry Reveals Binding Interactions of SARS-CoV-2 PLpro with Inhibitors and Cellular Targets
Virginia James, Rianna Godula, Jessica Perez, et al.
ACS Infectious Diseases (2024)
Closed Access | Times Cited: 1
Advances in the Search for SARS-CoV-2 Mpro and PLpro Inhibitors
Marcel Arruda Diogo, Augusto Gomes Teixeira Cabral, Renata Barbosa de Oliveira
Pathogens (2024) Vol. 13, Iss. 10, pp. 825-825
Open Access | Times Cited: 1
Potency Prediction of Covalent Inhibitors against SARS-CoV-2 3CL-like Protease and Multiple Mutants by Multiscale Simulations
Muya Xiong, Tianqing Nie, Zhewen Li, et al.
Journal of Chemical Information and Modeling (2024)
Closed Access | Times Cited: 1
Mutational Profiling of SARS-CoV-2 PLpro in human cells reveals requirements for function, structure, and drug escape
Xinyu Wu, Margareta Go, Julie V. Nguyen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Covalent DNA-Encoded Library Workflow Drives Discovery of SARS-CoV-2 Nonstructural Protein Inhibitors
Xudong Wang, Liwei Xiong, Ying Zhu, et al.
Journal of the American Chemical Society (2024)
Closed Access
Lycorine esters exert anti-HCoV-OC43 effect through reversibly acylating cysteine residue in the nsp 12 NiRAN domain
Yuheng Mei, Zhihui Yu, Yue Gong, et al.
Bioorganic Chemistry (2024) Vol. 154, pp. 108086-108086
Closed Access
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