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:

Thiazolidine-2,4-dione derivatives as potential α-glucosidase inhibitors: Synthesis, inhibitory activity, binding interaction and hypoglycemic activity
Mengyue Li, Jinping Sun, Bingwen Liang, et al.
Bioorganic Chemistry (2024) Vol. 144, pp. 107177-107177
Closed Access | Times Cited: 24

Showing 24 citing articles:

Novel thiosemicarbazide-based β-carboline derivatives as α-glucosidase inhibitors: Synthesis and biological evaluation
Bingwen Liang, Di Xiao, Shao‐Hua Wang, et al.
European Journal of Medicinal Chemistry (2024) Vol. 275, pp. 116595-116595
Closed Access | Times Cited: 22

New C-linked diarylheptanoid dimers as potential α-glucosidase inhibitors evidenced by biological, spectral and theoretical approaches
Xinyu Li, Tian Wang, Sheng‐Li Wu, et al.
International Journal of Biological Macromolecules (2025) Vol. 295, pp. 139496-139496
Closed Access

Design, 3D-QSAR, molecular docking, MD simulations, ADME/Tox properties and DFT study of benzimidazole derivatives as promising α-glucosidase inhibitors
Ayoub Khaldan, Soukaina Bouamrane, Mohamed Ouabane, et al.
Journal of Molecular Structure (2025) Vol. 1328, pp. 141351-141351
Closed Access

Synthesis, single crystal XRD, in vitro evaluation, molecular docking and ADMET studies of cuminaldehyde-thiazolidine-2,4-dione hybrids as potential α-glucosidase inhibitors
Abhik Paul, Sai Satyaprakash Mishra, Arnab Sarkar, et al.
Journal of Molecular Structure (2025), pp. 141510-141510
Closed Access

Novel sulfonyl hydrazide based β-carboline derivatives as potential α-glucosidase inhibitors: design, synthesis, and biological evaluation
Jinping Sun, Di Xiao, Ming Lang, et al.
Molecular Diversity (2024)
Closed Access | Times Cited: 3

Inhibition mechanism investigation of quercetagetin as a potential tyrosinase inhibitor
Faliang Liang
Frontiers in Chemistry (2024) Vol. 12
Open Access | Times Cited: 2

Investigation on the anti-α-glucosidase mechanism of aspergillus triazolate A from Oxalis corniculate L.
Qianqian Feng, Wei Yang, Xue Ma, et al.
International Journal of Biological Macromolecules (2024) Vol. 279, pp. 135457-135457
Closed Access | Times Cited: 2

Honokiol as an α-glucosidase inhibitor
Hua Zhu, Xin Zhong
Frontiers in Pharmacology (2024) Vol. 15
Open Access | Times Cited: 1

Alpha- glucosidase inhibition analysis and in silico studies of new tetrahydroquinazolin-4(1H)-one derivatives
Azadeh Tajmir-Riahi, Mohammad Hosein Sayahi, Mohammad Nazari Montazer, et al.
Results in Chemistry (2024) Vol. 9, pp. 101669-101669
Open Access | Times Cited: 1

Rosa × damascena Herrm. essential oil: anti-tyrosinase activity and phytochemical composition
Qiuyan Wu, Wanting Fang, Hao Liu, et al.
Frontiers in Pharmacology (2024) Vol. 15
Open Access | Times Cited: 1

Novel coumarin-thiazolidine-2,4-dione hybrids as potential α-glucosidase inhibitors: Synthesis and bioactivity evaluation
Bingwen Liang, Jianping Li, Simin Wu, et al.
Journal of Molecular Structure (2024), pp. 140481-140481
Closed Access | Times Cited: 1

Magnetic ligand fishing protocol combined with HPLC-FT-ICR-MS for screening potential α-Glucosidase inhibitors from UCG and in silico analysis
Bo Yuan, Yumeng Zhang, Xinting Man, et al.
Arabian Journal of Chemistry (2024) Vol. 17, Iss. 9, pp. 105899-105899
Open Access

Comprehensive exploration of a traditional Chinese medicinal plant of Magnolia officinalis based on high-coverage mass spectrometry and multidimensional chemical-biological analysis
Wenyu Wang, Ya‐Mei Song, Jia-Nuo Zhang, et al.
Journal of Chromatography B (2024) Vol. 1246, pp. 124290-124290
Closed Access

2β-Acetoxyferruginol derivatives as α-glucosidase inhibitors: Synthesis and biological evaluation
Yujia Zhou, Hengtong Qu, Xia Qiao, et al.
Bioorganic Chemistry (2024) Vol. 152, pp. 107770-107770
Closed Access

New oligomeric terpenoids fused with an oxazoline ring linkage from cones of Taxodium ascendens and their biological activities
Wenli Wang, Qi Gao, Jianqi Wei, et al.
Journal of Molecular Structure (2024), pp. 140206-140206
Closed Access

Insights into inhibitory action and interaction of bisdemethoxycurcumin on tyrosinase: Spectroscopic and docking analysis
Xiaofeng Min, Zhicheng Su, Huan Zhou, et al.
International Journal of Biological Macromolecules (2024) Vol. 281, pp. 136655-136655
Closed Access

Identification of new structure of indol-3-acetyl-arylsulfonohydrazide as potent α-glucosidase and α-amylase inhibitors and molecular docking
Muhammad Taha, Fazal Rahim, Khalid Zaman, et al.
Journal of Molecular Structure (2024) Vol. 1323, pp. 140719-140719
Closed Access

Novel rhodanine-thiazole hybrids as potential antidiabetic agents: A structure-based drug design approach
Shankar Gharge, Shankar G. Alegaon, Shriram D. Ranade, et al.
RSC Medicinal Chemistry (2024)
Closed Access

Acquiring stereospecific new pseudosugars: Obtaining rac-decahydro-1,4-epoxynaphthalene-2,3,5,6,7,8-hexaols from the Diels-Alder reaction and investigating their biological effects
Gökay Aydın, Canan Çakır Çoban, Namudar İzzet Kurbanoğlu, et al.
Bioorganic Chemistry (2024) Vol. 154, pp. 108078-108078
Closed Access

New benzimidazole–indole–amide derivatives as potent α‐glucosidase and acetylcholinesterase inhibitors
Narges Naimi, Somaye Karimian, Navid Dastyafteh, et al.
Archiv der Pharmazie (2024) Vol. 358, Iss. 1
Closed Access

Design, synthesis and biological evaluation of a 1,2,3-triazolyl-bearing betulinic acid derivatives as α-glucosidase inhibitors
Yufei Zhang, Jingjing Liu, Jiangyi Li, et al.
Journal of Molecular Structure (2024), pp. 141252-141252
Closed Access

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