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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.

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Showing 1-25 of 96 citing articles:

Reverse engineering Lewy bodies: how far have we come and how far can we go?
Mohamed Bilal Fares, Somanath Jagannath, Hilal A. Lashuel
Nature reviews. Neuroscience (2021) Vol. 22, Iss. 2, pp. 111-131
Closed Access | Times Cited: 140
The subcellular arrangement of alpha-synuclein proteoforms in the Parkinson’s disease brain as revealed by multicolor STED microscopy
Tim E. Moors, Christina A. Maat, Daniel Niedieker, et al.
Acta Neuropathologica (2021)
Open Access | Times Cited: 115
Neuropathology of incidental Lewy body & prodromal Parkinson’s disease
Thomas Koeglsperger, S Rumpf, Patricia Schließer, et al.
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 58
Artificial intelligence–coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases
Deepthy Kavungal, Pedro Magalhães, Senthil T. Kumar, et al.
Science Advances (2023) Vol. 9, Iss. 28
Open Access | Times Cited: 47
Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology
Magdalena I. Ivanova, Yuxi Lin, Young‐Ho Lee, et al.
Biophysical Chemistry (2020) Vol. 269, pp. 106507-106507
Open Access | Times Cited: 129
How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology
Senthil T. Kumar, Somanath Jagannath, Cindy François, et al.
Neurobiology of Disease (2020) Vol. 146, pp. 105086-105086
Open Access | Times Cited: 126
In situ architecture of neuronal α-Synuclein inclusions
Victoria A. Trinkaus, Irene Riera-Tur, Antonio Martínez-Sánchez, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 97
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: 79
Monitoring α-synuclein aggregation
Juan Estaun-Panzano, Marie-Laure Arotçarena, Erwan Bézard
Neurobiology of Disease (2022) Vol. 176, pp. 105966-105966
Open Access | Times Cited: 48
Physiological roles of α-synuclein serine-129 phosphorylation – not an oxymoron
Nagendran Ramalingam, Christian Haass, Ulf Dettmer
Trends in Neurosciences (2024) Vol. 47, Iss. 7, pp. 480-490
Closed Access | Times Cited: 8
Interactions of α-synuclein oligomers with lipid membranes
Greta Musteikytė, Akhila K. Jayaram, Catherine K. Xu, et al.
Biochimica et Biophysica Acta (BBA) - Biomembranes (2020) Vol. 1863, Iss. 4, pp. 183536-183536
Open Access | Times Cited: 61
The Convergence of Alpha-Synuclein, Mitochondrial, and Lysosomal Pathways in Vulnerability of Midbrain Dopaminergic Neurons in Parkinson’s Disease
Georgia Minakaki, Dimitri Krainc, Lena F. Burbulla
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 52
Altered ceramide metabolism is a feature in the extracellular vesicle-mediated spread of alpha-synuclein in Lewy body disorders
Marzena Kurzawa‐Akanbi, Seshu R. Tammireddy, Ivo Fabrik, et al.
Acta Neuropathologica (2021) Vol. 142, Iss. 6, pp. 961-984
Open Access | Times Cited: 42
In situ proximity labeling identifies Lewy pathology molecular interactions in the human brain
Bryan A. Killinger, Lee Marshall, Diptaman Chatterjee, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 5
Open Access | Times Cited: 33
The role of glycogen synthase kinase 3 beta in neurodegenerative diseases
Honglu Yu, Min Xiong, Zhentao Zhang
Frontiers in Molecular Neuroscience (2023) Vol. 16
Open Access | Times Cited: 20
Lewy body radius growth: The hypothesis of the cube root of time dependency
A. V. Kuznetsov
Journal of Theoretical Biology (2024) Vol. 581, pp. 111734-111734
Open Access | Times Cited: 7
Interaction of Alpha-Synuclein With Lipids: Mitochondrial Cardiolipin as a Critical Player in the Pathogenesis of Parkinson’s Disease
Valentina Gilmozzi, Giovanna Gentile, Maria Paulina Castelo Rueda, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 45
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
Cerebral dopamine neurotrophic factor reduces α-synuclein aggregation and propagation and alleviates behavioral alterations in vivo
Katrina Albert, Diana Pelizzari Raymundo, Anne Panhelainen, et al.
Molecular Therapy (2021) Vol. 29, Iss. 9, pp. 2821-2840
Open Access | Times Cited: 35
The roles of connectivity and neuronal phenotype in determining the pattern of α-synuclein pathology in Parkinson's disease
Michael X. Henderson, Martin T. Henrich, Fanni F. Geibl, et al.
Neurobiology of Disease (2022) Vol. 168, pp. 105687-105687
Open Access | Times Cited: 25
The association of lipids with amyloid fibrils
John M. Sanderson
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102108-102108
Open Access | Times Cited: 25
Calpain activation and progression of inflammatory cycles in Parkinson’s disease
Andrew Gao, Hannah M. McCoy, Vandana Zaman, et al.
Frontiers in Bioscience-Landmark (2022) Vol. 27, Iss. 1
Open Access | Times Cited: 24
Glucocerebrosidase activity and lipid levels are related to protein pathologies in Parkinson’s disease
Cheryl E. G. Leyns, Alice Prigent, Brenna Beezhold, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 14
α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson’s disease
Annie J. Zalon, Drew J. Quiriconi, Caleb Pitcairn, et al.
The Neuroscientist (2024) Vol. 30, Iss. 5, pp. 612-635
Closed Access | Times Cited: 5
α-Synuclein interaction with POPC/POPS vesicles.
Marija Dubackic, Veronica Lattanzi, Yun Liu, et al.
Soft Matter (2025)
Open Access
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