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:

Role of aberrant phase separation in pathological protein aggregation
Pijush Chakraborty, Markus Zweckstetter
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102678-102678
Closed Access | Times Cited: 38

Showing 1-25 of 38 citing articles:

The roles of intrinsically disordered proteins in neurodegeneration
Kagistia Hana Utami, Satoru Morimoto, Yasue Mitsukura, et al.
Biochimica et Biophysica Acta (BBA) - General Subjects (2025), pp. 130772-130772
Open Access | Times Cited: 2

Deciphering the role of liquid-liquid phase separation in sarcoma: Implications for pathogenesis and treatment
Zehao Cheng, Hua Wang, Y M Zhang, et al.
Cancer Letters (2025) Vol. 616, pp. 217585-217585
Closed Access | Times Cited: 2

The prolyl oligopeptidase and α-synuclein connection revisited
Roos Van Elzen, Yannick Waumans, Sangeeta Nath, et al.
Biochimie (2025)
Closed Access | Times Cited: 1

Intrinsic factors behind long COVID: IV. Hypothetical roles of the SARS‐CoV‐2 nucleocapsid protein and its liquid–liquid phase separation
Ahmed Eltayeb, Faisal Al‐Sarraj, Mona G. Alharbi, et al.
Journal of Cellular Biochemistry (2024) Vol. 125, Iss. 3
Closed Access | Times Cited: 9

β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein
Xi Li, Linwei Yu, Xikai Liu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 7

Membraneless organelles in health and disease: exploring the molecular basis, physiological roles and pathological implications
Yangxin Li, Brian Liu, Xi‐Yong Yu, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 6

Serum amyloid A binding to glycosaminoglycans is synergistic with amyloid formation: Therapeutic targeting in the inflammation-linked amyloidosis
Shobini Jayaraman, Angela Urdaneta, Marcus Fändrich, et al.
Journal of Molecular Biology (2025), pp. 169007-169007
Closed Access

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

Caffeine Inhibits Tau Aggregation and Destabilizes the Fibril Associated with Chronic Traumatic Encephalopathy: A REST2 and Conventional MD Simulations Study
Jiaxing Tang, Zhengdong Xu, Feng Wang, et al.
Journal of Chemical Information and Modeling (2025)
Closed Access

Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins
Jinyao Ji, Kui Xu, Wenjuan Wang, et al.
The Journal of Physical Chemistry Letters (2025), pp. 3553-3561
Closed Access

Phase Separation and Prion‐Like Aggregation of p53 Family Tumor Suppressors: From Protein Evolution to Cancer Treatment
Jerson L. Silva, Guilherme C. de Andrade, Elaine C. Petronilho, et al.
Journal of Neurochemistry (2025) Vol. 169, Iss. 4
Closed Access

Low-complexity domains in phase-separated droplets suppress the amyloid formation of yeast prion Sup35
Yumiko Ohhashi, Suguru Nishinami, Kentaro Shiraki, et al.
Deleted Journal (2025) Vol. 2, Iss. 1
Open Access

Assessing amyloid fibrils and amorphous aggregates: A review
Shaik Basha, Darshan Chikkanayakanahalli Mukunda, Aparna Pai, et al.
International Journal of Biological Macromolecules (2025), pp. 143725-143725
Open Access

Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation
Radost Waszkiewicz, Agnieszka Michaś, Michał K. Białobrzewski, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 19, pp. 5024-5033
Open Access | Times Cited: 3

The Proteomic Analysis of Cancer-Related Alterations in the Human Unfoldome
Victor Paromov, Vladimir N. Uversky, Ayorinde Cooley, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 3, pp. 1552-1552
Open Access | Times Cited: 2

Tannic acid as a biphasic modulator of tau protein liquid–liquid phase separation
Jiani Xiang, Jingxin Chen, Yanqing Liu, et al.
International Journal of Biological Macromolecules (2024) Vol. 275, pp. 133578-133578
Closed Access | Times Cited: 2

Exploring the Impact of Physiological C-Terminal Truncation on α-Synuclein Conformations to Unveil Mechanisms Regulating Pathological Aggregation
Fengjuan Huang, Jiajia Yan, Huan Xu, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 22, pp. 8616-8627
Closed Access | Times Cited: 2

Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health
Valerie Uytterhoeven, Patrik Verstreken, Eliana Nachman
The Journal of Cell Biology (2024) Vol. 224, Iss. 2
Closed Access | Times Cited: 2

Epigenetics in the formation of pathological aggregates in amyotrophic lateral sclerosis
Verónica Noches, Danae Campos-Melo, Cristian A. Droppelmann, et al.
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 1

Targeting Protein Aggregation: the Promising Application of Polyoxometalates in Neurodegenerative Diseases
Junyi Chen, Wenzhu Yang, Huilan Chen, et al.
Inorganic Chemistry Frontiers (2024)
Closed Access | Times Cited: 1

Deciphering the Monomeric and Dimeric Conformational Landscapes of the Full-Length TDP-43 and the Impact of the C-Terminal Domain
Vaishnavi Tammara, Abhilasha A. Doke, Santosh Kumar Jha, et al.
ACS Chemical Neuroscience (2024)
Closed Access | Times Cited: 1

Beyond BioID: Streptavidin outcompetes antibody fluorescence signals in protein localization and readily visualises targets evading immunofluorescence detection
Johanna Odenwald, Bernardo Gabiatti, Silke Braune, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation
Radost Waszkiewicz, Agnieszka Michaś, Michał K. Białobrzewski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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