
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:
Endogenous Levels of Alpha-Synuclein Modulate Seeding and Aggregation in Cultured Cells
Eftychia Vasili, Antonio Dominguez‐Meijide, Manuel Flores‐León, et al.
Molecular Neurobiology (2022) Vol. 59, Iss. 2, pp. 1273-1284
Open Access | Times Cited: 30
Eftychia Vasili, Antonio Dominguez‐Meijide, Manuel Flores‐León, et al.
Molecular Neurobiology (2022) Vol. 59, Iss. 2, pp. 1273-1284
Open Access | Times Cited: 30
Showing 1-25 of 30 citing articles:
A topographical atlas of α-synuclein dosage and cell type-specific expression in adult mouse brain and peripheral organs
Haley Geertsma, Zoe Fisk, Lillian Sauline, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 16
Haley Geertsma, Zoe Fisk, Lillian Sauline, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 16
Research Priorities on the Role of α‐Synuclein in Parkinson's Disease Pathogenesis
Jacqueline Burré, Robert H. Edwards, Glenda M. Halliday, et al.
Movement Disorders (2024) Vol. 39, Iss. 10, pp. 1663-1678
Open Access | Times Cited: 9
Jacqueline Burré, Robert H. Edwards, Glenda M. Halliday, et al.
Movement Disorders (2024) Vol. 39, Iss. 10, pp. 1663-1678
Open Access | Times Cited: 9
Fasudil inhibits α-synuclein aggregation through ROCK-inhibition-mediated mechanisms
Lucia Lage, Ana I. Rodríguez‐Pérez, José L. Labandeira‐García, et al.
Neurotherapeutics (2025), pp. e00544-e00544
Open Access | Times Cited: 1
Lucia Lage, Ana I. Rodríguez‐Pérez, José L. Labandeira‐García, et al.
Neurotherapeutics (2025), pp. e00544-e00544
Open Access | Times Cited: 1
Aggregation of alpha-synuclein disrupts mitochondrial metabolism and induce mitophagy via cardiolipin externalization
Olivier Lurette, Rebeca Martín-Jiménez, Mehtab Khan, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 11
Open Access | Times Cited: 20
Olivier Lurette, Rebeca Martín-Jiménez, Mehtab Khan, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 11
Open Access | Times Cited: 20
Neuronal constitutive endolysosomal perforations enable α-synuclein aggregation by internalized PFFs
Anwesha Sanyal, Gustavo Scanavachi, Elliott Somerville, et al.
The Journal of Cell Biology (2024) Vol. 224, Iss. 2
Closed Access | Times Cited: 5
Anwesha Sanyal, Gustavo Scanavachi, Elliott Somerville, et al.
The Journal of Cell Biology (2024) Vol. 224, Iss. 2
Closed Access | Times Cited: 5
Synaptic location is a determinant of the detrimental effects of α-synuclein pathology to glutamatergic transmission in the basolateral amygdala
Liqiang Chen, Chetan Nagaraja, Samuel Daniels, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 22
Liqiang Chen, Chetan Nagaraja, Samuel Daniels, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 22
Extracellular alpha-synuclein: Sensors, receptors, and responses
Renato Domingues, Ricardo Sant’Anna, Anna Carolina Carvalho da Fonseca, et al.
Neurobiology of Disease (2022) Vol. 168, pp. 105696-105696
Open Access | Times Cited: 21
Renato Domingues, Ricardo Sant’Anna, Anna Carolina Carvalho da Fonseca, et al.
Neurobiology of Disease (2022) Vol. 168, pp. 105696-105696
Open Access | Times Cited: 21
Constitutive Endolysosomal Perforation in Neurons allows Induction of alpha-Synuclein Aggregation by Internalized Pre-Formed Fibrils
Anwesha Sanyal, Gustavo Scanavachi, Elliott Somerville, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Anwesha Sanyal, Gustavo Scanavachi, Elliott Somerville, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
A high-fidelity microfluidic platform reveals retrograde propagation as the main mechanism of α-Synuclein spread in human neurons
Rozan Vroman, Lorenzo de Lichtervelde, Karamjit Singh Dolt, et al.
npj Parkinson s Disease (2025) Vol. 11, Iss. 1
Open Access
Rozan Vroman, Lorenzo de Lichtervelde, Karamjit Singh Dolt, et al.
npj Parkinson s Disease (2025) Vol. 11, Iss. 1
Open Access
miR-101a-3p Impairs Synaptic Plasticity and Contributes to Synucleinopathy
Mary Xylaki, Isabel Paiva, Mohammed Al-Azzani, et al.
Journal of Parkinson s Disease (2023) Vol. 13, Iss. 2, pp. 179-196
Open Access | Times Cited: 10
Mary Xylaki, Isabel Paiva, Mohammed Al-Azzani, et al.
Journal of Parkinson s Disease (2023) Vol. 13, Iss. 2, pp. 179-196
Open Access | Times Cited: 10
⍺-Synuclein levels in Parkinson's disease – Cell types and forms that contribute to pathogenesis
Giselle T. Sagredo, Onur Tanglay, Shrey Shahdadpuri, et al.
Experimental Neurology (2024) Vol. 379, pp. 114887-114887
Open Access | Times Cited: 3
Giselle T. Sagredo, Onur Tanglay, Shrey Shahdadpuri, et al.
Experimental Neurology (2024) Vol. 379, pp. 114887-114887
Open Access | Times Cited: 3
α‐Synuclein Pathology Spreads in a Midbrain–Hindbrain Assembloid Model
Gemma Gomez‐Giro, Daniela Frangenberg, Diana Alejandra Méndez Vega, et al.
Advanced Science (2025)
Open Access
Gemma Gomez‐Giro, Daniela Frangenberg, Diana Alejandra Méndez Vega, et al.
Advanced Science (2025)
Open Access
The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains
Samuel Peña‐Díaz, Jordi Pujols, Eftychia Vasili, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 5, pp. 101902-101902
Open Access | Times Cited: 13
Samuel Peña‐Díaz, Jordi Pujols, Eftychia Vasili, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 5, pp. 101902-101902
Open Access | Times Cited: 13
Alpha Synuclein Toxicity and Non-Motor Parkinson’s
G. Mazzotta, Carmela Conte
Cells (2024) Vol. 13, Iss. 15, pp. 1265-1265
Open Access | Times Cited: 2
G. Mazzotta, Carmela Conte
Cells (2024) Vol. 13, Iss. 15, pp. 1265-1265
Open Access | Times Cited: 2
Modelling α-Synuclein Aggregation and Neurodegeneration with Fibril Seeds in Primary Cultures of Mouse Dopaminergic Neurons
Aurore Tourville, David Akbar, Olga Corti, et al.
Cells (2022) Vol. 11, Iss. 10, pp. 1640-1640
Open Access | Times Cited: 10
Aurore Tourville, David Akbar, Olga Corti, et al.
Cells (2022) Vol. 11, Iss. 10, pp. 1640-1640
Open Access | Times Cited: 10
Neuroprotective effects of isatin and afobazole in rats with rotenone-induced Parkinsonism are accompanied by increased brain levels of Triton X-100 soluble alpha-synuclein
О.А. Бунеева, И. Г. Капица, Victor G. Zgoda, et al.
Biomeditsinskaya Khimiya (2023) Vol. 69, Iss. 5, pp. 290-299
Open Access | Times Cited: 6
О.А. Бунеева, И. Г. Капица, Victor G. Zgoda, et al.
Biomeditsinskaya Khimiya (2023) Vol. 69, Iss. 5, pp. 290-299
Open Access | Times Cited: 6
The mycobiota-gut-brain axis in Parkinson's disease: A review on what we know and what paths we can still take to advance this field of study
Dionísio Pedro Amorim Neto, Anderson S. Sant’Ana
Fungal Biology Reviews (2023) Vol. 46, pp. 100327-100327
Open Access | Times Cited: 5
Dionísio Pedro Amorim Neto, Anderson S. Sant’Ana
Fungal Biology Reviews (2023) Vol. 46, pp. 100327-100327
Open Access | Times Cited: 5
IGF2 prevents dopaminergic neuronal loss and decreases intracellular alpha-synuclein accumulation in Parkinson’s disease models
Javiera Arcos, Felipe Grünenwald, Denisse Sepúlveda, et al.
Cell Death Discovery (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 5
Javiera Arcos, Felipe Grünenwald, Denisse Sepúlveda, et al.
Cell Death Discovery (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 5
Neuroprotective Effects of a Novel Demeclocycline Derivative Lacking Antibiotic Activity: From a Hit to a Promising Lead Compound
Rodrigo Hernán Tomas‐Grau, Florencia González‐Lizárraga, Diego Ploper, et al.
Cells (2022) Vol. 11, Iss. 17, pp. 2759-2759
Open Access | Times Cited: 8
Rodrigo Hernán Tomas‐Grau, Florencia González‐Lizárraga, Diego Ploper, et al.
Cells (2022) Vol. 11, Iss. 17, pp. 2759-2759
Open Access | Times Cited: 8
Alpha Synuclein Toxicity and Non-motor Parkinson’s
G. Mazzotta, Carmela Conte
(2024)
Open Access | Times Cited: 1
G. Mazzotta, Carmela Conte
(2024)
Open Access | Times Cited: 1
Epigenetic Alterations of Cognition Functions in Parkinson's Disease
Fatemeh Hasani, Payam Ahmadi, Mahdi Masrour, et al.
(2024)
Open Access | Times Cited: 1
Fatemeh Hasani, Payam Ahmadi, Mahdi Masrour, et al.
(2024)
Open Access | Times Cited: 1
Monitoring α-synuclein Aggregation Induced by Preformed α-synuclein Fibrils in an In Vitro Model System
Beom Jin Kim, Hye Rin Noh, Hyongjun Jeon, et al.
Experimental Neurobiology (2023) Vol. 32, Iss. 3, pp. 147-156
Open Access | Times Cited: 3
Beom Jin Kim, Hye Rin Noh, Hyongjun Jeon, et al.
Experimental Neurobiology (2023) Vol. 32, Iss. 3, pp. 147-156
Open Access | Times Cited: 3
Neuroprotective Effects of a Novel Demeclocycline Derivative Lacking Antibiotic Activity: From a Hit to a Promising Lead Compound
Rodrigo Hernán Tomas‐Grau, Florencia González‐Lizárraga, Diego Ploper, et al.
(2022)
Open Access | Times Cited: 4
Rodrigo Hernán Tomas‐Grau, Florencia González‐Lizárraga, Diego Ploper, et al.
(2022)
Open Access | Times Cited: 4
Glycation of alpha-synuclein enhances aggregation and neuroinflammatory responses
Eftychia Vasili, Annekatrin König, Mohammed Al-Azzani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Eftychia Vasili, Annekatrin König, Mohammed Al-Azzani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging
Parasuraman Swaminathan, Therése Klingstedt, Vasileios Theologidis, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 22, pp. 12458-12458
Open Access
Parasuraman Swaminathan, Therése Klingstedt, Vasileios Theologidis, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 22, pp. 12458-12458
Open Access