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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:

Liquid–liquid phase separation of full-length prion protein initiates conformational conversion in vitro
Hiroya Tange, Daisuke Ishibashi, Takehiro Nakagaki, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100367-100367
Open Access | Times Cited: 52

Showing 1-25 of 52 citing articles:

Amyloid formation as a protein phase transition
Thomas C. T. Michaels, Daoyuan Qian, Anđela Šarić, et al.
Nature Reviews Physics (2023) Vol. 5, Iss. 7, pp. 379-397
Closed Access | Times Cited: 83
Spatiotemporal modulations in heterotypic condensates of prion and α-synuclein control phase transitions and amyloid conversion
Aishwarya Agarwal, Lisha Arora, K. Sandeep, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 72
Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands
Elaine C. Petronilho, Murilo M. Pedrote, Mayra A. Marques, et al.
Chemical Science (2021) Vol. 12, Iss. 21, pp. 7334-7349
Open Access | Times Cited: 76
An intrinsically disordered pathological prion variant Y145Stop converts into self-seeding amyloids via liquid–liquid phase separation
Aishwarya Agarwal, K. Sandeep, Anamika Avni, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 45
Open Access | Times Cited: 74
Manganese promotes α-synuclein amyloid aggregation through the induction of protein phase transition
Bingkuan Xu, Shuai Huang, Yinghui Liu, et al.
Journal of Biological Chemistry (2021) Vol. 298, Iss. 1, pp. 101469-101469
Open Access | Times Cited: 60
Calcium promotes α-synuclein liquid-liquid phase separation to accelerate amyloid aggregation
Shuai Huang, Bingkuan Xu, Yinghui Liu
Biochemical and Biophysical Research Communications (2022) Vol. 603, pp. 13-20
Closed Access | Times Cited: 40
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: 39
Targeting Biomolecular Condensation and Protein Aggregation against Cancer
Jerson L. Silva, Débora Foguel, Vı́tor F. Ferreira, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9094-9138
Closed Access | Times Cited: 37
Liquid-liquid phase separation of the prion protein is regulated by the octarepeat domain independently of histidines and copper
Janine Kamps, Verian Bader, Konstanze F. Winklhofer, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107310-107310
Open Access | Times Cited: 10
Copper drives prion protein phase separation and modulates aggregation
Mariana Juliani do Amaral, Satabdee Mohapatra, Aline Ribeiro Passos, et al.
Science Advances (2023) Vol. 9, Iss. 44
Open Access | Times Cited: 19
Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications
Niccolò Candelise, Silvia Scaricamazza, Illari Salvatori, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 11, pp. 6016-6016
Open Access | Times Cited: 41
Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation
Jerson L. Silva, Tuane C. R. G. Vieira, Yraima Cordeiro, et al.
Current Opinion in Structural Biology (2022) Vol. 73, pp. 102346-102346
Closed Access | Times Cited: 23
Liquid–liquid phase separation induced by crowding condition affects amyloid-β aggregation mechanism
Ryuki Kobayashi, Hideki Nabika
Soft Matter (2024) Vol. 20, Iss. 27, pp. 5331-5342
Closed Access | Times Cited: 5
The N-terminal domain of the prion protein is required and sufficient for liquid–liquid phase separation: A crucial role of the Aβ-binding domain
Janine Kamps, Yu-Hsuan Lin, Rosario Oliva, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 1, pp. 100860-100860
Open Access | Times Cited: 31
Prion Protein Biology Through the Lens of Liquid-Liquid Phase Separation
Aishwarya Agarwal, Samrat Mukhopadhyay
Journal of Molecular Biology (2021) Vol. 434, Iss. 1, pp. 167368-167368
Closed Access | Times Cited: 28
Ser392 phosphorylation modulated a switch between p53 and transcriptional condensates
Zhuojun Dai, Guoli Li, Qunyang Chen, et al.
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms (2022) Vol. 1865, Iss. 4, pp. 194827-194827
Closed Access | Times Cited: 19
Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance
Doris Loh, Russel J. Reıter
Molecules (2022) Vol. 27, Iss. 3, pp. 705-705
Open Access | Times Cited: 18
Modulation of biomolecular phase behavior by metal ions
Katarzyna Sołtys, Aneta Tarczewska, Dominika Bystranowska
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2023) Vol. 1870, Iss. 8, pp. 119567-119567
Open Access | Times Cited: 10
Chaperone-Mediated Heterotypic Phase Separation Prevents the Amyloid Formation of the Pathological Y145Stop Prion Protein Variant
Lisha Arora, Dipankar Bhowmik, Snehasis Sarkar, et al.
Journal of Molecular Biology (2025) Vol. 437, Iss. 5, pp. 168955-168955
Closed Access
Accelerated amyloid fibril formation at the interface of liquid–liquid phase‐separated droplets by depletion interactions
K. Yamaguchi, Joji Mima, Kichitaro Nakajima, et al.
Protein Science (2025) Vol. 34, Iss. 2
Open Access
Mechanism of amyloid fibril formation triggered by breakdown of supersaturation
Keiichi Yamaguchi, Kichitaro Nakajima, Hirotsugu Ogi, et al.
Deleted Journal (2025) Vol. 2, Iss. 1
Open Access
Excess PrPC inhibits muscle cell differentiation via miRNA-enhanced liquid–liquid phase separation implicated in myopathy
Jing Tao, Yanping Zeng, Bin Dai, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
The prion protein and its ligands: Insights into structure-function relationships
Mohsin Shafiq, Stefano Da Vela, Ladan Amin, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2022) Vol. 1869, Iss. 6, pp. 119240-119240
Open Access | Times Cited: 14
Phase separation of the mammalian prion protein: Physiological and pathological perspectives
Mariana Juliani do Amaral, Maria Heloisa O. Freire, Marcius S. Almeida, et al.
Journal of Neurochemistry (2022) Vol. 166, Iss. 1, pp. 58-75
Open Access | Times Cited: 13
Development of α-Synuclein Real-Time Quaking-Induced Conversion as a Diagnostic Method for α-Synucleinopathies
Takehiro Nakagaki, Noriyuki Nishida, Katsuya Satoh
Frontiers in Aging Neuroscience (2021) Vol. 13
Open Access | Times Cited: 16
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