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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.

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Showing 1-25 of 34 citing articles:

Liquid–liquid phase separation in tumor biology
Xuhui Tong, Rong Tang, Jin Xu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 142
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 | Times Cited: 3
Combating deleterious phase transitions in neurodegenerative disease
April L. Darling, James Shorter
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2021) Vol. 1868, Iss. 5, pp. 118984-118984
Open Access | Times Cited: 81
Role of condensates in modulating DNA repair pathways and its implication for chemoresistance
Giuseppe Dall’Agnese, Alessandra Dall’Agnese, Salman F. Banani, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 6, pp. 104800-104800
Open Access | Times Cited: 28
Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS
Maria Tsekrekou, Μαρία Γιαννάκου, Katerina Papanikolopoulou, et al.
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 14
Phase separation and pathologic transitions of RNP condensates in neurons: implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders
Aditi Naskar, Asima Nayak, Muthu Raj Salaikumaran, et al.
Frontiers in Molecular Neuroscience (2023) Vol. 16
Open Access | Times Cited: 23
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: 22
Study liquid–liquid phase separation with optical microscopy: A methodology review
Xiufeng Zhang, Haoyang Li, Yue Ma, et al.
APL Bioengineering (2023) Vol. 7, Iss. 2
Open Access | Times Cited: 20
Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises
Luke McAlary, Yee Lian Chew, Jeremy S. Lum, et al.
Frontiers in Cellular Neuroscience (2020) Vol. 14
Open Access | Times Cited: 38
Targeting TDP‐43 proteinopathy with drugs and drug‐like small molecules
Emanuele Buratti
British Journal of Pharmacology (2020) Vol. 178, Iss. 6, pp. 1298-1315
Open Access | Times Cited: 35
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: 4
One‐pot synthesis of tunable fluorescent polyethylene glycol (PEG) polymer for antimicrobial and anticancer theranostics
Dokkari Nagalaxmi Yadav, Dinesh Harijan, Sunil Venkanna Pogu, et al.
MedComm – Biomaterials and Applications (2025) Vol. 4, Iss. 1
Open Access
Predicting Mito-Target Interactions for Per-and Poly-Fluoroalkyl Compounds: Mapping Mitochondrial Toxicity on Zebrafish Voltage-Dependent Anion Channel 2
Michael González‐Durruthy, Amit Kumar Halder, Ana S. Moura, et al.
Aquatic Toxicology (2025) Vol. 281, pp. 107302-107302
Closed Access
Roles of RNA-binding proteins in neurological disorders, COVID-19, and cancer
Daniel Ruben Akiola Sanya, Claudia Cava, Djamila Onésime
Human Cell (2022) Vol. 36, Iss. 2, pp. 493-514
Open Access | Times Cited: 15
Prion-like Spreading of Disease in TDP-43 Proteinopathies
Emma Pongrácová, Emanuele Buratti, Maurizio Romano
Brain Sciences (2024) Vol. 14, Iss. 11, pp. 1132-1132
Open Access | Times Cited: 3
The Regulation of TDP-43 Structure and Phase Transitions: A Review
Yanqing Liu, Jiani Xiang, Hang Gong, et al.
The Protein Journal (2025)
Closed Access
Phase Separation: Orchestrating Biological Adaptations to Environmental Fluctuations
Wenxiu Wang, F.‐S. HAN, Zhi Qi, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 10, pp. 4614-4614
Open Access
Challenges and Discoveries in Polypharmacology of Neurodegenerative Diseases
Luciana Scotti, Teresa Carolliny Moreira Lustoza Rodrigues, Natália Ferreira de Sousa, et al.
Current Topics in Medicinal Chemistry (2023) Vol. 23, Iss. 5, pp. 349-370
Closed Access | Times Cited: 8
Elevated constitutive expression of Hsp40 chaperone Sis1 reduces TDP-43 aggregation-induced oxidative stress in Ire1 pathway dependent-manner in yeast TDP-43 proteinopathy model of amyotrophic lateral sclerosis
Vidhya Bharathi, Akarsh Bajpai, Irene Tomy Parappuram, et al.
Biochemical and Biophysical Research Communications (2022) Vol. 595, pp. 28-34
Closed Access | Times Cited: 12
Curcumin inhibits liquid–liquid phase separation of fused in sarcoma and attenuates the sequestration of pyruvate kinase to restore cellular metabolism
Wen‐Pu Shi, W. Lin, Wan‐Yi Ge, et al.
Food & Function (2023) Vol. 14, Iss. 10, pp. 4621-4631
Closed Access | Times Cited: 7
Protein phase separation: A novel therapy for cancer?
Wei Wang, Yingqian Chen, Aixiao Xu, et al.
British Journal of Pharmacology (2020) Vol. 177, Iss. 22, pp. 5008-5030
Open Access | Times Cited: 17
Role of CNC1 gene in TDP-43 aggregation-induced oxidative stress-mediated cell death in S. cerevisiae model of ALS
Vidhya Bharathi, Amandeep Girdhar, Basant K. Patel
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2021) Vol. 1868, Iss. 6, pp. 118993-118993
Open Access | Times Cited: 14
Zn2+ modulates in vitro phase separation of TDP-432C and mutant TDP-432C-A315T C-terminal fragments of TDP-43 protein implicated in ALS and FTLD-TDP diseases
Preethi Saravanan, Vidhya Bharathi, Basant K. Patel
International Journal of Biological Macromolecules (2021) Vol. 176, pp. 186-200
Closed Access | Times Cited: 10
Computational Insights Into the Mechanism of EGCG's Binding and Inhibition of the TDP‐43 Aggregation
Vini D. Meshram, Ramkumar Balaji, Preethi Saravanan, et al.
Chemical Biology & Drug Design (2024) Vol. 104, Iss. 4
Closed Access | Times Cited: 1
Phosphorylated TAR DNA-binding protein-43: Aggregation and antibody-based inhibition
Josephine Esposto, Sanela Martić
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2021) Vol. 1867, Iss. 12, pp. 166234-166234
Closed Access | Times Cited: 7
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