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:

Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH
Samuel Dada, Maarten C. Hardenberg, Zenon Toprakcioglu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 9
Open Access | Times Cited: 54

Showing 1-25 of 54 citing articles:

Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
Giulio Tesei, Kresten Lindorff‐Larsen
Open Research Europe (2023) Vol. 2, pp. 94-94
Open Access | Times Cited: 81

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: 81

Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu
Manisha Poudyal, Komal Patel, Laxmikant Gadhe, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 72

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: 65

Molecular Crowding: The History and Development of a Scientific Paradigm
Caterina Alfano, Yann Fichou, Klaus Huber, et al.
Chemical Reviews (2024) Vol. 124, Iss. 6, pp. 3186-3219
Open Access | Times Cited: 37

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: 24

Molecular mechanisms of amyloid formation in living systems
Tessa Sinnige
Chemical Science (2022) Vol. 13, Iss. 24, pp. 7080-7097
Open Access | Times Cited: 41

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: 36

VAMP2 regulates phase separation of α-synuclein
Aishwarya Agarwal, Aswathy Chandran, Farheen Raza, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 8, pp. 1296-1308
Open Access | Times Cited: 12

Protein–protein interactions regulating α-synuclein pathology
Jiannan Wang, Lijun Dai, Sichun Chen, et al.
Trends in Neurosciences (2024) Vol. 47, Iss. 3, pp. 209-226
Closed Access | Times Cited: 11

Pharmacological inhibition of α-synuclein aggregation within liquid condensates
Samuel Dada, Zenon Toprakcioglu, Mariana P. Cali, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 11

Towards sequence-based principles for protein phase separation predictions
Michele Vendruscolo, Mónika Fuxreiter
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102317-102317
Open Access | Times Cited: 21

α-Synuclein liquid condensates fuel fibrillar α-synuclein growth
Leonard Piroska, Alexis Fenyi, Scott E. Thomas, et al.
Science Advances (2023) Vol. 9, Iss. 33
Open Access | Times Cited: 17

Single-photon microscopy to study biomolecular condensates
Eleonora Perego, Sabrina Zappone, Francesco Castagnetti, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 16

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: 6

Tau forms synaptic nano-biomolecular condensates controlling the dynamic clustering of recycling synaptic vesicles
Shanley F. Longfield, Mahdie Mollazade, Tristan P. Wallis, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 16

Molecular Insights into Aggrephagy: Their Cellular Functions in the Context of Neurodegenerative Diseases
Valentín Cóppola-Segovia, Fulvio Reggiori
Journal of Molecular Biology (2024) Vol. 436, Iss. 15, pp. 168493-168493
Open Access | Times Cited: 5

DNA Framework–Programmed Nanoscale Enzyme Assemblies
Nan Cao, Ruiyan Guo, Ping Song, et al.
Nano Letters (2024) Vol. 24, Iss. 15, pp. 4682-4690
Closed Access | Times Cited: 5

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

Aggregation mechanisms and molecular structures of amyloid‐β in Alzheimer’s disease
Zheng Niu, Xinrui Gui, Shuang Feng, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 48
Open Access | Times Cited: 4

Molecular Insights into α-Synuclein Fibrillation: A Raman Spectroscopy and Machine Learning Approach
Nathan Coles, Suzan Elsheikh, Agathe Quesnel, et al.
ACS Chemical Neuroscience (2025)
Closed Access

A novel alpha-synuclein K58N missense variant in a patient with Parkinson's disease
Mohammed Al-Azzani, Sandrina Weber, Nagendran Ramalingam, et al.
medRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

Aggregation of α-synuclein splice isoforms through a phase separation pathway
Alexander Röntgen, Zenon Toprakcioglu, Samuel Dada, et al.
Science Advances (2025) Vol. 11, Iss. 16
Closed Access

Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation
Barend O. W. Elenbaas, Lucie Khemtémourian, J. Antoinette Killian, et al.
Biochemistry (2022) Vol. 61, Iss. 14, pp. 1465-1472
Open Access | Times Cited: 18

Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts
Robert I. Horne, Michael A. Metrick, Wing K. Man, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 17, pp. 3125-3131
Open Access | Times Cited: 10

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