ArticlePloS one2013
Wildtype and A30P mutant alpha-synuclein form different fibril structures.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Genetics of α-Synuclein: The Prime Pathological Player of Parkinson's Disease.Neurotoxicity research · 2026Review
- Effect of hydrogen sulfide on alpha-synuclein aggregation and cell viability.Scientific reports · 2025Article
- Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.Journal of molecular biology · 2022Review
- Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils.Biomolecules · 2022Article
- Consequences of variability in α-synuclein fibril structure on strain biology.Acta neuropathologica · 2022Review
- A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics.Chemical science · 2021Article
- Metal ions shape α-synuclein.Scientific reports · 2020Article
- Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro.Molecules (Basel, Switzerland) · 2020Article
- Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity.Protein engineering, design & selection : PEDS · 2019Article
- Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species.Scientific reports · 2019Article
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- Alpha-synuclein stepwise aggregation reveals features of an early onset mutation in Parkinson's disease.Communications biology · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- Non-steric-zipper models for pathogenic α-synuclein conformers.APL bioengineering · 2018Article
- Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein.Chemical communications (Cambridge, England) · 2018Article
- Article
- Alpha-synuclein overexpression in the olfactory bulb initiates prodromal symptoms and pathology of Parkinson's disease.Translational neurodegeneration · 2018Article
- C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets.Journal of the American Chemical Society · 2017Article
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
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Authors and funding
13 authors.
Funding
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Abstract
Parkinson's Disease (PD) is a neurodegenerative movement disorder affecting millions of people worldwide. One of the key players in the development of the disease is the protein α-synuclein (aSN), which aggregates in the brain of PD patients. The aSN mutant A30P has been reported to cause early-onset familial PD and shows different aggregation behavior compared to wt aSN. Here we use a multidisciplinary approach to compare the aggregation process of wt and A30P aSN. In agreement with previous studies, we observe an initial lag phase followed by a continuous structural development of fibrils until reaching an apparent monomer-aggregate equilibrium state and a plateau in Thioflavin T (ThT) fluorescence intensity. However, at later timepoints A30P shows greater propensity than αSN wt to form dense bundled fibril networks. Combining small angle x-ray scattering, x-ray fibre diffraction and linear dichroism, we demonstrate that while the microscopic structure of the individual fibril essentially remains constant throughout the experiment, the formation of dense A30P fibril networks occur through a continuous assembly pathway while the formation of less dense wt fibril networks with fewer contact points follows a continuous path during the elongation phase and a second rearrangement phase after reaching the ThT fluorescence plateau. Our work thus highlights that structural rearrangements proceed beyond the plateau in ThT-based monitoring of the fibrillation process, and the density and morphology of the resulting fibril networks is highly dependent on the aSN form studied.
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