ArticleJournal of structural biology2019
Comparison of the 3D structures of mouse and human α-synuclein fibrils by solid-state NMR and STEM.
Article in Journal of structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Engineering functional ventral midbrain dopaminergic neurons in human organoids through WNT modulation and bioreactor culture.Molecular psychiatry · 2026Article
- Propagation of α-synuclein pathology: models, mechanisms and future goals.Molecular neurodegeneration advances · 2026Review
- Synaptic Vesicle Disruption in Parkinson's Disease: Dual Roles of α-Synuclein and Emerging Therapeutic Targets.Brain sciences · 2025Review
- Synaptic vesicle-omics in mice captures signatures of aging and synucleinopathy.Nature communications · 2025Article
- Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.Science advances · 2024Article
- Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.Scientific reports · 2023Article
- Molecular Insights into the Misfolding and Dimerization Dynamics of the Full-Length α-Synuclein from Atomistic Discrete Molecular Dynamics Simulations.ACS chemical neuroscience · 2022Article
- Different α-synuclein prion strains cause dementia with Lewy bodies and multiple system atrophy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Collusion of α-Synuclein and Aβ aggravating co-morbidities in a novel prion-type mouse model.Molecular neurodegeneration · 2021Article
- Therapeutic Potential ofParkinson's disease · 2021Review
- Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.Molecular neurodegeneration · 2020Article
- Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid-State NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2020Article
- The emerging role of α-synuclein truncation in aggregation and disease.The Journal of biological chemistry · 2020Review
- Carboxy-terminal truncations of mouse α-synuclein alter aggregation and prion-like seeding.FEBS letters · 2020Article
- Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation.Neural regeneration research · 2020Review
- Review
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8 authors.
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Abstract
Intra-neuronal aggregation of α-synuclein into fibrils is the molecular basis for α-synucleinopathies, such as Parkinson's disease. The atomic structure of human α-synuclein (hAS) fibrils was recently determined by Tuttle et al. using solid-state NMR (ssNMR). The previous study found that hAS fibrils are composed of a single protofilament. Here, we have investigated the structure of mouse α-synuclein (mAS) fibrils by STEM and isotope-dilution ssNMR experiments. We found that in contrast to hAS, mAS fibrils consist of two or even three protofilaments which are connected by rather weak interactions in between them. Although the number of protofilaments appears to be different between hAS and mAS, we found that they have a remarkably similar secondary structure and protofilament 3D structure as judged by secondary chemical shifts and intra-molecular distance restraints. We conclude that the two mutant sites between hAS and mAS (positions 53 and 87) in the fibril core region are crucial for determining the quaternary structure of α-synuclein fibrils.
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