Frontiers | Alpha-Synuclein Pathology and the Role of the Microbiota in Parkinson's Disease | Neuroscience
Alpha-synuclein stepwise aggregation reveals features of an early onset mutation in Parkinson's disease | Communications Biology
Sorting out release, uptake and processing of alpha‐synuclein during prion‐like spread of pathology - Tyson - 2016 - Journal of Neurochemistry - Wiley Online Library
Phenotypic manifestation of α-synuclein strains derived from Parkinson's disease and multiple system atrophy in human dopaminergic neurons | Nature Communications
Discriminating α-synuclein strains in Parkinson's disease and multiple system atrophy | Nature
CLR01 protects dopaminergic neurons in vitro and in mouse models of Parkinson's disease | Nature Communications
Parkinson's disease and multiple system atrophy have distinct α-synuclein seed characteristics - Journal of Biological Chemistry
IJMS | Free Full-Text | Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease | HTML
Evidence of distinct α-synuclein strains underlying disease heterogeneity | SpringerLink
Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity | Scientific Reports
Neurodegenerative diseases distinguished through protein-structure analysis
CMT-3 targets different α-synuclein aggregates mitigating their toxic and inflammogenic effects | Scientific Reports
α-synuclein strains that cause distinct pathologies differentially inhibit proteasome | eLife
Anti-amyloid Compounds Inhibit α-Synuclein Aggregation Induced by Protein Misfolding Cyclic Amplification (PMCA)* - Journal of Biological Chemistry
Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation Lucas HR, Fernández RD - Neural Regen Res
IJMS | Free Full-Text | The Role of α-Synuclein Oligomers in Parkinson's Disease | HTML
α-Synuclein strains target distinct brain regions and cell types | Nature Neuroscience
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity | PNAS
Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons: Cell
Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies - ScienceDirect
α-synuclein strains that cause distinct pathologies differentially inhibit proteasome | eLife
Spread of α-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis | Nature Neuroscience
α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies | Nature Medicine
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel | Nature Communications
α-synuclein strains that cause distinct pathologies differentially inhibit proteasome | eLife
