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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:

Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies
Maarten C. Hardenberg, Tessa Sinnige, Sam Casford, et al.
Journal of Molecular Cell Biology (2020)
Open Access | Times Cited: 89

Showing 1-25 of 89 citing articles:

Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
Giulio Tesei, Thea K. Schulze, Ramón Crehuet, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 44
Open Access | Times Cited: 291
Widespread occurrence of the droplet state of proteins in the human proteome
Maarten C. Hardenberg, Attila Horváth, Viktor Ambrus, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 52, pp. 33254-33262
Open Access | Times Cited: 286
Fluorescent Nanoparticles for Super-Resolution Imaging
Wei Li, Gabriele S. Kaminski Schierle, Bingfu Lei, et al.
Chemical Reviews (2022) Vol. 122, Iss. 15, pp. 12495-12543
Open Access | Times Cited: 165
Generic nature of the condensed states of proteins
Mónika Fuxreiter, Michele Vendruscolo
Nature Cell Biology (2021) Vol. 23, Iss. 6, pp. 587-594
Closed Access | Times Cited: 126
Modulating α-Synuclein Liquid–Liquid Phase Separation
Ajay Singh Sawner, Soumik Ray, Preeti Yadav, et al.
Biochemistry (2021) Vol. 60, Iss. 48, pp. 3676-3696
Closed Access | Times Cited: 114
Post-translational modifications in liquid-liquid phase separation: a comprehensive review
Jingxian Li, Mengdi Zhang, Weirui Ma, et al.
Molecular Biomedicine (2022) Vol. 3, Iss. 1
Open Access | Times Cited: 103
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: 83
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: 79
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: 68
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: 58
Stress-related biomolecular condensates in plants
Jorge Solís-Miranda, Monika Chodasiewicz, Aleksandra Skirycz, et al.
The Plant Cell (2023) Vol. 35, Iss. 9, pp. 3187-3204
Open Access | Times Cited: 48
The role of biomolecular condensates in protein aggregation
Brent S. Visser, Wojciech P. Lipiński, Evan Spruijt
Nature Reviews Chemistry (2024) Vol. 8, Iss. 9, pp. 686-700
Closed Access | Times Cited: 27
Sequence Determinants of the Aggregation of Proteins Within Condensates Generated by Liquid-liquid Phase Separation
Michele Vendruscolo, Mónika Fuxreiter
Journal of Molecular Biology (2021) Vol. 434, Iss. 1, pp. 167201-167201
Open Access | Times Cited: 101
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
Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation
Emil G. P. Stender, Soumik Ray, Rasmus K. Norrild, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 61
Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau
Pablo Gracia, David Polanco, Jorge Tarancón-Díez, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 52
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
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
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: 29
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: 15
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: 15
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: 14
VAMP2 chaperones α-synuclein in synaptic vesicle co-condensates
Chuchu Wang, Kai Zhang, Bin Cai, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 8, pp. 1287-1295
Closed Access | Times Cited: 14
Emerging experimental methods to study the thermodynamics of biomolecular condensate formation
Soumik Ray, Alexander K. Buell
The Journal of Chemical Physics (2024) Vol. 160, Iss. 9
Open Access | Times Cited: 9
The role of water in the primary nucleation of protein amyloid aggregation
José D. Camino, Pablo Gracia, Nunilo Cremades
Biophysical Chemistry (2020) Vol. 269, pp. 106520-106520
Open Access | Times Cited: 62
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