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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 Role of Lipids in the Initiation of α-Synuclein Misfolding
Martin Kiechle, Veselin Grozdanov, Karin M. Danzer
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

α-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia
Lia‐Raluca Olari, Sichen Liu, Franziska Arnold, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2
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: 27
α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques
Nicolò Bisi, Lucia Feni, Kaliroi Peqini, et al.
Frontiers in Chemistry (2021) Vol. 9
Open Access | Times Cited: 50
The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates
Mikhail Matveyenka, Stanislav Rizevsky, Dmitry Kurouski
FEBS Letters (2022) Vol. 596, Iss. 11, pp. 1424-1433
Open Access | Times Cited: 34
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
Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Laxmikant Gadhe, Arunima Sakunthala, Semanti Mukherjee, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106736-106736
Closed Access | Times Cited: 39
Cell Death via Lipid Peroxidation and Protein Aggregation Diseases
Katsuya Iuchi, Tomoka Takai, Hisashi Hisatomi
Biology (2021) Vol. 10, Iss. 5, pp. 399-399
Open Access | Times Cited: 36
The role of the PLA2G6 gene in neurodegenerative diseases
Xinyue Deng, Lamei Yuan, Joseph Jankovic, et al.
Ageing Research Reviews (2023) Vol. 89, pp. 101957-101957
Closed Access | Times Cited: 14
Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson’s disease-related fibril polymorphism
Chi‐Jing Choong, César Aguirre, Keita Kakuda, et al.
Acta Neuropathologica (2023) Vol. 145, Iss. 5, pp. 573-595
Open Access | Times Cited: 13
Peripheral Upregulation of Parkinson’s Disease-Associated Genes Encoding α-Synuclein, β-Glucocerebrosidase, and Ceramide Glucosyltransferase in Major Depression
Razvan-Marius Brazdis, Claudia von Zimmermann, Bernd Lenz, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 6, pp. 3219-3219
Open Access | Times Cited: 5
Small molecule modulators of Alpha-Synuclein Aggregation and Toxicity: Pioneering an Emerging Arsenal Against Parkinson’s Disease
Ishfaq Ahmad Ahanger, Tanveer Ali Dar
Ageing Research Reviews (2024) Vol. 101, pp. 102538-102538
Closed Access | Times Cited: 5
Anti-Parkinson Effects of Holothuria leucospilota-Derived Palmitic Acid in Caenorhabditis elegans Model of Parkinson’s Disease
Tanatcha Sanguanphun, Sukrit Promtang, Nilubon Sornkaew, et al.
Marine Drugs (2023) Vol. 21, Iss. 3, pp. 141-141
Open Access | Times Cited: 13
Molecular mechanism of α-synuclein aggregation on lipid membranes revealed
Alexander J. Dear, Xiangyu Teng, Sarah R. Ball, et al.
Chemical Science (2024) Vol. 15, Iss. 19, pp. 7229-7242
Open Access | Times Cited: 4
Salt-Induced Membrane-Bound Conformation of the NAC Domain of α-Synuclein Leads to Structural Polymorphism of Amyloid Fibrils
Ryota Imaura, Koichi Matsuo
Biomolecules (2025) Vol. 15, Iss. 4, pp. 506-506
Open Access
Synaptic vesicle-omics in mice captures signatures of aging and synucleinopathy
Virginia Gao, Julita Chlebowicz, Kerry Gaskin, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Innovative treatment targeting gangliosides aimed at blocking the formation of neurotoxic α-synuclein oligomers in Parkinson’s disease
Nouara Yahi, Coralie Di Scala, Henri Chahinian, et al.
Glycoconjugate Journal (2021) Vol. 39, Iss. 1, pp. 1-11
Closed Access | Times Cited: 24
Exploring glycolytic enzymes in disease: potential biomarkers and therapeutic targets in neurodegeneration, cancer and parasitic infections
Maura Rojas-Pirela, Diego Andrade-Alviárez, Verónica Rojas, et al.
Open Biology (2025) Vol. 15, Iss. 2
Open Access
Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils
A. Frese, Cody Goode, Kiryl Zhaliazka, et al.
Protein Science (2023) Vol. 32, Iss. 8
Open Access | Times Cited: 9
α-Synuclein at the Presynaptic Axon Terminal as a Double-Edged Sword
Li Yang Tan, Kwan Hou Tang, Lynette Yu You Lim, et al.
Biomolecules (2022) Vol. 12, Iss. 4, pp. 507-507
Open Access | Times Cited: 14
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
Lipid level alteration in human and cellular models of alpha synuclein mutations
Hila Avisar, Cristina Guardia‐Laguarta, Matthew Surface, et al.
npj Parkinson s Disease (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 12
Integrated metabolomics and proteomics analysis of plasma lipid metabolism in Parkinson’s disease
Paulina Gątarek, Joanna Kałużna‐Czaplińska
Expert Review of Proteomics (2024) Vol. 21, Iss. 1-3, pp. 13-25
Closed Access | Times Cited: 2
Ultrastructural diversity of alpha-Synuclein pathology in the post-mortem brain of Parkinson patients: implications for Lewy Body formation
Amanda J. Lewis, Lukas van den Heuvel, Marta Di Fabrizio, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Cu2+ ions modulate the interaction between α-synuclein and lipid membranes
Hongzhi Wang, Cecilia Mörman, Rebecca Sternke‐Hoffmann, et al.
Journal of Inorganic Biochemistry (2022) Vol. 236, pp. 111945-111945
Open Access | Times Cited: 9
Untwisted α-Synuclein Filaments Formed in the Presence of Lipid Vesicles
Anvesh K. R. Dasari, Lucas Dillard, Sujung Yi, et al.
Biochemistry (2022) Vol. 61, Iss. 17, pp. 1766-1773
Open Access | Times Cited: 9
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