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:

Acetylcholinesterase: A Versatile Template to Coin Potent Modulators of Multiple Therapeutic Targets
F. Javier Luque, Diego Muñoz‐Torrero
Accounts of Chemical Research (2024)
Open Access | Times Cited: 14

Showing 14 citing articles:

Bioactivity, cytotoxicity, and molecular modeling studies of novel sulfonamides as dual inhibitors of carbonic anhydrases and acetylcholinesterase
Özcan Güleç, Cüneyt Türkeş, Mustafa Arslan, et al.
Journal of Molecular Liquids (2024) Vol. 410, pp. 125558-125558
Closed Access | Times Cited: 23

Rapid screening of acetylcholinesterase inhibitors in Qi-Fu-Yin using magnetic metal–organic frameworks immobilized with acetylcholinesterase
Hengyu Li, Hongwei Zhao, Lingxiao Chen, et al.
Bioorganic Chemistry (2025) Vol. 156, pp. 108183-108183
Closed Access

Analysis of skeletal diversity of multi-target directed ligands (MTDLs) targeting Alzheimer’s disease
Uzma Azam, Muhammad Moazzam Naseer, Christophe Rochais
European Journal of Medicinal Chemistry (2025) Vol. 286, pp. 117277-117277
Open Access

New 1,2,3-triazole-quinazolinone skeleton as potential cholinesterase and α-amylase inhibitors: In vitro and in silico studies
Esra Erdoğan, Özge Güngör, Seyit Ali Güngör, et al.
Journal of Molecular Liquids (2025) Vol. 424, pp. 126986-126986
Closed Access

In Silico Study, Synthesis, and In Vitro Evaluation of Nicotinamide-Substituted 1,3,5-Triazine Derivatives as Inhibitors of Acetylcholinesterase and Butyrylcholinesterase
Tutumoni Kalita, Shampa Dutta, Anshul Shakya, et al.
Journal of Molecular Structure (2025), pp. 141577-141577
Closed Access

Phytomolecules as Alzheimer’s Therapeutics: A Comprehensive Review
Mohd Kamil Hussain, Mafaz Ahmad, Shahnaaz Khatoon, et al.
European Journal of Medicinal Chemistry (2025) Vol. 288, pp. 117401-117401
Closed Access

Synthesis of novel hybrids of 1,2,3-triazoles-hydrazone: targeting cholinesterases and Alzheimer's related genes
Diba Shareghi-Boroujeni, Aida Iraji, Mahintaj Dara, et al.
Future Medicinal Chemistry (2024) Vol. 16, Iss. 15, pp. 1519-1535
Closed Access | Times Cited: 1

Harnessing the Therapeutic Potential of Peptides for Synergistic Treatment of Alzheimer’s Disease by Targeting Aβ Aggregation, Metal-Mediated Aβ Aggregation, Cholinesterase, Tau Degradation, and Oxidative Stress
Kamaljot Singh, Anupamjeet Kaur, Bhupesh Goyal, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 14, pp. 2545-2564
Closed Access | Times Cited: 1

Identification of a Novel Inhibitor of Cimex lectularius Acetylcholinesterase
Juan Qin, Zhiguang Yuchi
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 22, pp. 12498-12507
Closed Access

Spatiotemporal Communication in Artificial Cell Consortia for Dynamic Control of DNA Nanostructures
Antoni Llopis‐Lorente, Jingxin Shao, Jordi Ventura, et al.
ACS Central Science (2024) Vol. 10, Iss. 8, pp. 1619-1628
Open Access

Targeting Alzheimer's Disease with Novel Dual-Function 3,5-diaryl-4,5-dihydro-1H-pyrazole-1-carbothioamide derivatives
Aikaterini Katsogiannou, Danai Karta, Antonio Di Stefano, et al.
European Journal of Medicinal Chemistry Reports (2024), pp. 100235-100235
Open Access

Biological Implications of the Intrinsic Deformability of Human Acetylcholinesterase Induced by Diverse Compounds: A Computational Study
Ysaías J. Alvarado, Lenin González-Paz, J. L. Paz, et al.
Biology (2024) Vol. 13, Iss. 12, pp. 1065-1065
Open Access

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