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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:

Curcumin Interacts with α-Synuclein Condensates To Inhibit Amyloid Aggregation under Phase Separation
Bingkuan Xu, Jing Chen, Yinghui Liu
ACS Omega (2022) Vol. 7, Iss. 34, pp. 30281-30290
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

Mass photometric detection and quantification of nanoscale α-synuclein phase separation
Soumik Ray, Thomas O. Mason, Lars Boyens‐Thiele, et al.
Nature Chemistry (2023) Vol. 15, Iss. 9, pp. 1306-1316
Open Access | Times Cited: 60
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 20
Structure–Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates
Serene W. Chen, Joseph D. Barritt, Roberta Cascella, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 15, pp. 10537-10549
Open Access | Times Cited: 14
Synucleins: New Data on Misfolding, Aggregation and Role in Diseases
Andrei Surguchov, Alexei Surguchev
Biomedicines (2022) Vol. 10, Iss. 12, pp. 3241-3241
Open Access | Times Cited: 44
Development of Small Molecules Targeting α-Synuclein Aggregation: A Promising Strategy to Treat Parkinson’s Disease
Samuel Peña‐Díaz, Javier García‐Pardo, Salvador Ventura
Pharmaceutics (2023) Vol. 15, Iss. 3, pp. 839-839
Open Access | Times Cited: 26
Liquid–liquid phase separation of α‐synuclein is highly sensitive to sequence complexity
Anindita Mahapatra, Robert W. Newberry
Protein Science (2024) Vol. 33, Iss. 4
Open Access | Times Cited: 7
Gut–Brain Axis in Focus: Polyphenols, Microbiota, and Their Influence on α-Synuclein in Parkinson’s Disease
Elizabeth Riegelman, Kathy S. Xue, Jia-Sheng Wang, et al.
Nutrients (2024) Vol. 16, Iss. 13, pp. 2041-2041
Open Access | Times Cited: 7
Distinct Effects of Familial Parkinson’s Disease-Associated Mutations on α-Synuclein Phase Separation and Amyloid Aggregation
Bingkuan Xu, Fengshuo Fan, Yunpeng Liu, et al.
Biomolecules (2023) Vol. 13, Iss. 5, pp. 726-726
Open Access | Times Cited: 19
Small molecules in regulating protein phase separation
Siyang Li, Yanyan Wang, Luhua Lai
Acta Biochimica et Biophysica Sinica (2023) Vol. 55, Iss. 7, pp. 1075-1083
Open Access | Times Cited: 16
Aquaporin-4 and Parkinson’s Disease
К. В. Лапшина, И. В. Екимова
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 3, pp. 1672-1672
Open Access | Times Cited: 6
Emerging regulatory mechanisms and functions of biomolecular condensates: implications for therapeutic targets
Soyoung Jeon, Yong‐Duck Chung, Jae‐Sung Lim, et al.
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access
Curcumin reverses cognitive deficits through promoting neurogenesis and synapse plasticity via the upregulation of PSD95 and BDNF in mice
Gaifen Li, Qiong Wu, Chao Wang, et al.
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access
Spatiotemporal Dynamic Monitoring of Protein Conformation Changes by Super-resolution Imaging
Wei Yu, He Xuan, Jiabao Fang, et al.
Dyes and Pigments (2025) Vol. 236, pp. 112689-112689
Closed Access
Neuro-Nutraceutical Polyphenols: How Far Are We?
Maria Teresa Gentile, Iolanda Camerino, Loredana F. Ciarmiello, et al.
Antioxidants (2023) Vol. 12, Iss. 3, pp. 539-539
Open Access | Times Cited: 13
Curcumin Inhibits α-Synuclein Aggregation by Acting on Liquid–Liquid Phase Transition
Jian-Feng Li, Zi-Qun Jiang, Sen Cao, et al.
Foods (2024) Vol. 13, Iss. 9, pp. 1287-1287
Open Access | Times Cited: 4
Aggregation and phase separation of α-synuclein in Parkinson’s disease
W. Han, Mengrui Wei, Fei Xu, et al.
Chemical Communications (2024) Vol. 60, Iss. 52, pp. 6581-6590
Closed Access | Times Cited: 4
Regulation of Peptide Liquid–Liquid Phase Separation by Aromatic Amino Acid Composition
Amit Netzer, Avigail Baruch Leshem, Shirel Veretnik, et al.
Small (2024)
Open Access | Times Cited: 4
4-Arylidene curcumin derivatives in vitro inhibit α-Synuclein aggregation and disaggregate the preformed fibril
Wei Liu, Wei Zhang, Li-Zi Xing, et al.
Bioorganic & Medicinal Chemistry (2023) Vol. 96, pp. 117529-117529
Closed Access | Times Cited: 8
Biomolecular condensates and disease pathogenesis
Ke Ruan, Ge Bai, Yanshan Fang, et al.
Science China Life Sciences (2024) Vol. 67, Iss. 9, pp. 1792-1832
Closed Access | Times Cited: 2
Small Molecules, α-Synuclein Pathology, and the Search for Effective Treatments in Parkinson’s Disease
GianPietro Sechi, Maria Margherita Sechi
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 20, pp. 11198-11198
Open Access | Times Cited: 2
The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation
Oxana V. Galzitskaya, Sergei Y. Grishin, Anna V. Glyakina, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3781-3781
Open Access | Times Cited: 7
Navigating α‐Synuclein Aggregation Inhibition: Methods, Mechanisms, and Molecular Targets
Maksym Galkin, Anastasiia Priss, Yevhenii Kyriukha, et al.
The Chemical Record (2023) Vol. 24, Iss. 2
Closed Access | Times Cited: 6
Inhibition of α-Synuclein fibrillation by curcumin and difluoro boron derivatized curcumin complexes in aqueous environment
Tinku, Shaukat Ali M. Shaikh, K. Indira Priyadarsini, et al.
Journal of Molecular Liquids (2024) Vol. 405, pp. 125063-125063
Closed Access | Times Cited: 1
Liquid-liquid phase separation in human diseases: Functions, mechanisms and treatments
Tongqing Yue, Fei Zhang, Yanan Wei, et al.
Nano Today (2024) Vol. 59, pp. 102521-102521
Closed Access | Times Cited: 1
Degradation of pathogenic amyloids induced by matrix metalloproteinase-9
Olga V. Stepanenko, Maksim I. Sulatsky, Е. В. Михайлова, et al.
International Journal of Biological Macromolecules (2024) Vol. 281, pp. 136362-136362
Closed Access | Times Cited: 1
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