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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:

The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition
Wing K. Man, Islam Bogachan Tahirbegi, Michail D. Vrettas, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 86

Showing 1-25 of 86 citing articles:

Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 116
α-Synuclein fibrils subvert lysosome structure and function for the propagation of protein misfolding between cells through tunneling nanotubes
Aysegul Dilsizoglu Senol, Maura Samarani, Sylvie Syan, et al.
PLoS Biology (2021) Vol. 19, Iss. 7, pp. e3001287-e3001287
Open Access | Times Cited: 83
Alpha-Synuclein Post-translational Modifications: Implications for Pathogenesis of Lewy Body Disorders
Nelson de Oliveira Manzanza, Lucia Sedlackova, Raj N. Kalaria
Frontiers in Aging Neuroscience (2021) Vol. 13
Open Access | Times Cited: 61
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
Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases
Orkid Coskuner‐Weber, Ozan Mirzanli, Vladimir N. Uversky
Biophysical Reviews (2022) Vol. 14, Iss. 3, pp. 679-707
Open Access | Times Cited: 46
APOE4 exacerbates α-synuclein seeding activity and contributes to neurotoxicity in Alzheimer’s disease with Lewy body pathology
Yunjung Jin, Fuyao Li, Berkiye Sonoustoun, et al.
Acta Neuropathologica (2022) Vol. 143, Iss. 6, pp. 641-662
Open Access | Times Cited: 42
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
Lost in traffic: consequences of altered palmitoylation in neurodegeneration
Firyal Ramzan, Fatima Abrar, Gyana Gourab Mishra, et al.
Frontiers in Physiology (2023) Vol. 14
Open Access | Times Cited: 25
More than meets the eye in Parkinson’s disease and other synucleinopathies: from proteinopathy to lipidopathy
Manuel Flores‐León, Tiago F. Outeiro
Acta Neuropathologica (2023) Vol. 146, Iss. 3, pp. 369-385
Open Access | Times Cited: 25
Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson’s Disease
Kamil Saramowicz, Natalia Siwecka, Grzegorz Galita, et al.
International Journal of Molecular Sciences (2023) Vol. 25, Iss. 1, pp. 360-360
Open Access | Times Cited: 24
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: 14
Modulation of Gut Microbiota Through Dietary Intervention in Neuroinflammation and Alzheimer’s and Parkinson’s Diseases
Şerife Ayten, Saniye Bilici
Current Nutrition Reports (2024) Vol. 13, Iss. 2, pp. 82-96
Open Access | Times Cited: 13
Synuclein Regulates Synaptic Vesicle Clustering and Docking at a Vertebrate Synapse
Kaitlyn E. Fouke, M. Elizabeth Wegman, Sarah A. Weber, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 46
A necessary considering factor for breeding: growth-defense tradeoff in plants
Hong Zhang, Yuanming Liu, Xiangyu Zhang, et al.
Stress Biology (2023) Vol. 3, Iss. 1
Open Access | Times Cited: 20
The translational potential of cholesterol-based therapies for neurological disease
Marta Valenza, Giulia Birolini, Elena Cattaneo
Nature Reviews Neurology (2023) Vol. 19, Iss. 10, pp. 583-598
Closed Access | Times Cited: 19
Electrochemical Monitoring of Real‐Time Vesicle Dynamics Induced by Tau in a Confined Nanopipette
Kele Chen, Ru‐Jia Yu, Cheng-Bing Zhong, et al.
Angewandte Chemie International Edition (2024)
Closed Access | Times Cited: 7
Lipids shape brain function through ion channel and receptor modulations: physiological mechanisms and clinical perspectives
Salvatore Incontro, Maria Laura Musella, Malika Sammari, et al.
Physiological Reviews (2024) Vol. 105, Iss. 1, pp. 137-207
Closed Access | Times Cited: 7
Alpha-Synuclein and Lipids: The Elephant in the Room?
Alessia Sarchione, Antoine Marchand, Jean‐Marc Taymans, et al.
Cells (2021) Vol. 10, Iss. 9, pp. 2452-2452
Open Access | Times Cited: 40
Abnormal accumulation of lipid droplets in neurons induces the conversion of alpha-Synuclein to proteolytic resistant forms in a Drosophila model of Parkinson’s disease
Victor Girard, Florence Jollivet, Oskar Knittelfelder, et al.
PLoS Genetics (2021) Vol. 17, Iss. 11, pp. e1009921-e1009921
Open Access | Times Cited: 36
Altered conformation of α-synuclein drives dysfunction of synaptic vesicles in a synaptosomal model of Parkinson’s disease
Luis Fonseca‐Ornelas, Thibault Viennet, Matteo Rovere, et al.
Cell Reports (2021) Vol. 36, Iss. 1, pp. 109333-109333
Open Access | Times Cited: 33
The Role of Ubiquitin–Proteasome System and Mitophagy in the Pathogenesis of Parkinson's Disease
Liang Yú, Guangshang Zhong, Mingxin Ren, et al.
NeuroMolecular Medicine (2023) Vol. 25, Iss. 4, pp. 471-488
Closed Access | Times Cited: 16
Mechanisms of Glucocerebrosidase Dysfunction in Parkinson’s Disease
Diptaman Chatterjee, Dimitri Krainc
Journal of Molecular Biology (2023) Vol. 435, Iss. 12, pp. 168023-168023
Open Access | Times Cited: 15
In silico analysis of alpha‐synuclein protein variants and posttranslational modifications related to Parkinson's disease
A. N. R. Da Silva, Gabriel Rodrigues Coutinho Pereira, Luiz Felippe Sarmento Bonet, et al.
Journal of Cellular Biochemistry (2024) Vol. 125, Iss. 3
Closed Access | Times Cited: 5
Glycation of α-synuclein hampers its binding to synaptic-like vesicles and its driving effect on their fusion
Ana Belén Uceda, Juan Frau, Bartolomé Vilanova, et al.
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 6
Open Access | Times Cited: 20
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