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:

Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils
Kevin A. Murray, Carolyn J. Hu, Hope Pan, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 7
Open Access | Times Cited: 24

Showing 24 citing articles:

Caenorhabditis elegans as a Model System to Study Human Neurodegenerative Disorders
Antonis Roussos, Katerina Kitopoulou, Fivos Borbolis, et al.
Biomolecules (2023) Vol. 13, Iss. 3, pp. 478-478
Open Access | Times Cited: 31

Single‐Molecule Insight Into α‐Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds
Xiang Li, Lulu Bi, Shenqing Zhang, et al.
Advanced Science (2025)
Open Access | Times Cited: 1

D-peptide-magnetic nanoparticles fragment tau fibrils and rescue behavioral deficits in a mouse model of Alzheimer’s disease
Ke Hou, Hope Pan, Hedieh Shahpasand‐Kroner, et al.
Science Advances (2024) Vol. 10, Iss. 18
Open Access | Times Cited: 8

Amyloid accelerator polyphosphate fits as the mystery density in α-synuclein fibrils
Philipp Huettemann, P. R. Mahadevan, Justine Lempart, et al.
PLoS Biology (2024) Vol. 22, Iss. 10, pp. e3002650-e3002650
Open Access | Times Cited: 5

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: 11

Liganded magnetic nanoparticles for magnetic resonance imaging of α-synuclein
Hope Pan, Melinda Balbirnie, Ke Hou, et al.
npj Parkinson s Disease (2025) Vol. 11, Iss. 1
Open Access

Naringenin-Functionalized Gold Nanoparticles and Their Role in α-Synuclein Stabilization
Anupam Maity, Animesh Mondal, Shubham Kundu, et al.
Langmuir (2023) Vol. 39, Iss. 21, pp. 7231-7248
Closed Access | Times Cited: 9

Host-to-graft propagation of inoculated α-synuclein into transplanted human induced pluripotent stem cell-derived midbrain dopaminergic neurons
Serina Gima, Kazuya Oe, Kaneyasu Nishimura, et al.
Regenerative Therapy (2024) Vol. 25, pp. 229-237
Open Access | Times Cited: 3

Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases
Soumick Naskar, Nidhi Gour
Life (2023) Vol. 13, Iss. 7, pp. 1523-1523
Open Access | Times Cited: 7

Effect of Clemizole on Alpha-Synuclein-Preformed Fibrils-Induced Parkinson’s Disease Pathology: A Pharmacological Investigation
Bhupesh Vaidya, Pankaj Gupta, Soumojit Biswas, et al.
NeuroMolecular Medicine (2024) Vol. 26, Iss. 1
Closed Access | Times Cited: 2

E46K Mutation of α-Synuclein Preorganizes the Intramolecular Interactions Crucial for Aggregation
Defa Huang, Cong Guo
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 15, pp. 4803-4813
Closed Access | Times Cited: 6

Characterization of the pathogenic α-Synuclein Variant V15A in Parkinson´s disease
Sokhna Haissatou Diaw, Max Borsche, Linn Streubel-Gallasch, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 6

A natural small molecule‐mediated inhibition of alpha‐synuclein aggregation leads to neuroprotection in Caenorhabditis elegans
Tulika Srivastava, Divya Tyagi, Siraj Fatima, et al.
Journal of Neurochemistry (2023) Vol. 168, Iss. 8, pp. 1640-1654
Closed Access | Times Cited: 5

Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics
Sharif Arar, Md. Anzarul Haque, Rakez Kayed
Proteins Structure Function and Bioinformatics (2023)
Open Access | Times Cited: 5

Ultrastructures of α-Synuclein Filaments in Synucleinopathy Brains and Experimental Models
Airi Tarutani, Masato Hasegawa
Journal of Movement Disorders (2023) Vol. 17, Iss. 1, pp. 15-29
Open Access | Times Cited: 5

Development of small molecules for disrupting pathological amyloid aggregation in neurodegenerative diseases
Tianyi Cao, Xiang Li, Dan Li, et al.
Ageing and Neurodegenerative Diseases (2023) Vol. 3, Iss. 3
Open Access | Times Cited: 3

Chemical disaggregation of alpha-synuclein fibrils as a therapy for synucleinopathies
Shenjie Wu, Nancy C. Hernandez Villegas, Randy Schekman
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 11
Open Access | Times Cited: 2

Modelling α-synuclein processing in primary patient cells for pharmacological intervention
Jessica Smith, George D. Mellick, Alex M. Sykes
Exploration of Medicine (2023) Vol. 4, Iss. 5, pp. 695-708
Open Access | Times Cited: 1

Targeting Hydrophobic Residues in the Alpha-Synuclein NAC Domain Disrupts Aggregation and Seed-Competent Fibril Formation
Viswanath Das, Sayed Mostafa Modarres Mousavi, Narendran Annadurai, et al.
Research Square (Research Square) (2024)
Closed Access

Identification of α-Synuclein Aggregation Inhibitors via High-Throughput Screening
Samuel Peña‐Díaz, Zoe Manglano-Artuñedo, Francisca Pinheiro, et al.
Neuromethods (2024), pp. 61-85
Closed Access

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