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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:

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 26-50 of 54 citing articles:

HSPB6: A lipid-dependent molecular chaperone inhibits α-synuclein aggregation
Valentina Secco, Tatiana Tiago, Roxine Staats, et al.
iScience (2024) Vol. 27, Iss. 9, pp. 110657-110657
Open Access | Times Cited: 3
Liquid–liquid phase separation of alpha‐synuclein increases the structural variability of fibrils formed during amyloid aggregation
Mantas Žiaunys, Darius Šulskis, Dominykas Veiveris, et al.
FEBS Journal (2024) Vol. 291, Iss. 20, pp. 4522-4538
Open Access | Times Cited: 3
Pathological Involvement of Protein Phase Separation and Aggregation in Neurodegenerative Diseases
Y. Wu, Biao Ma, Chang Yu Liu, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 18, pp. 10187-10187
Open Access | Times Cited: 3
Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid–liquid phase separation
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 3
Inhibition of Protein Aggregation and Endoplasmic Reticulum Stress as a Targeted Therapy for α-Synucleinopathy
Natalia Siwecka, Kamil Saramowicz, Grzegorz Galita, et al.
Pharmaceutics (2023) Vol. 15, Iss. 8, pp. 2051-2051
Open Access | Times Cited: 8
Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores
Sarah E. Sandler, Robert I. Horne, Sara Rocchetti, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 47, pp. 25776-25788
Open Access | Times Cited: 8
Macromolecular Crowding Promotes Re-entrant Liquid–Liquid Phase Separation of Human Serum Transferrin and Prevents Surface-Induced Fibrillation
Chinmaya Kumar Patel, Chanchal Rani, Rajesh Kumar, et al.
Biomacromolecules (2023) Vol. 24, Iss. 8, pp. 3917-3928
Open Access | Times Cited: 6
Metal Ion-Induced Unusual Stability of the Metastable Vesicle-like Intermediates Evolving during the Self-Assembly of Phenylalanine: Prominent Role of Surface Charge Inversion
Debanjan Bagchi, Avijit Maity, Anjan Chakraborty
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 16, pp. 4468-4476
Closed Access | Times Cited: 2
The Role of Liquid‒Liquid Phase Separation in the Accumulation of Pathological Proteins: New Perspectives on the Mechanism of Neurodegenerative Diseases
Xingyu Lu, Jiongtong Lu, Shengnan Li, et al.
Aging and Disease (2024)
Open Access | Times Cited: 2
Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation
Michele Vendruscolo
Expert Opinion on Drug Discovery (2023) Vol. 18, Iss. 8, pp. 881-891
Open Access | Times Cited: 5
VAMP2 regulates phase separation of alpha-synuclein
Aishwarya Agarwal, Farheen Raza, Christine Hilcenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
Biosensing strategies for amyloid‐like protein aggregates
Yuhang Zhou, Shijun Yan, Wanting Dong, et al.
BMEMat (2023) Vol. 2, Iss. 1
Open Access | Times Cited: 4
A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation
Tommaso Amico, Samuel Dada, Andrea Lazzari, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 1
A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation
Tommaso Amico, Samuel Dada, Andrea Lazzari, et al.
(2024)
Open Access | Times Cited: 1
A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation
Tommaso Amico, Samuel Dada, Andrea Lazzari, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 1
Liquid-liquid phase separation of Tau and α-synuclein: a new pathway of overlapping neuropathologies
Leandro Cruz Rodríguez, Nahuel N. Foressi, M. Soledad Celej
Biochemical and Biophysical Research Communications (2024) Vol. 741, pp. 151053-151053
Closed Access | Times Cited: 1
A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation
Tommaso Amico, Samuel Dada, Andrea Lazzari, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
(Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation
Yraima Cordeiro, Maria Heloisa O. Freire, Adalgisa Felippe Wiecikowski, et al.
Biophysical Reviews (2023) Vol. 15, Iss. 4, pp. 577-589
Closed Access | Times Cited: 2
Aggregation of the Amyloid-β Peptide (Aβ40) within Condensates Generated through Liquid-Liquid Phase Separation
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Molecular mechanism of Alzheimer’s β-amyloid peptide aggregation
Yanyan Li, Xiwen Mao, Keyu Liu, et al.
Chinese Science Bulletin (Chinese Version) (2024)
Open Access
A scale-invariant log-normal droplet size distribution below the transition concentration for protein phase separation
Tommaso Amico, Samuel Dada, Andrea Lazzari, et al.
(2024)
Open Access
Identification of Glycerol 3-phosphate acyltransferase as a potent modifier of α-Synuclein-induced toxicity
Kah‐Leong Lim, Mengda Ren, Gui Yin Grace Lim, et al.
Research Square (Research Square) (2024)
Open Access
Screening of liquid–liquid phase separation conditions for proteins with a mixed solution kit of biomacromolecular crowding agents
Wan‐Yi Ge, Wen‐Pu Shi, Xueting Wang, et al.
Journal of Molecular Liquids (2024) Vol. 406, pp. 125038-125038
Closed Access
The N-terminal Region of α-Synuclein Controls Amyloid Nucleation at the Condensate Interface
Rebecca J. Thrush, Devkee M. Vadukul, Siân C. Allerton, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
The role of RNA in the nanoscale organization of alpha-synuclein phase separation
Sabrina Zappone, Eleonora Perego, Jakob Rupert, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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