ArticleThe Journal of biological chemistry2016
α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.BBA advances · 2026Review
- Tunable lipid-coated nanoporous silver sheet for characterization of protein-membrane interactions by surface-enhanced Raman scattering (SERS).Analytical and bioanalytical chemistry · 2023Article
- Aggregation of Disordered Proteins Associated with Neurodegeneration.International journal of molecular sciences · 2023Review
- 3,4-Dihydroxyphenylethanol and 3,4-dihydroxyphenylacetic acid affect the aggregation process of E46K variant of α-synuclein at different extent: Insights into the interplay between protein dynamics and catechol effect.Protein science : a publication of the Protein Society · 2022Article
- A Brain-Penetrant Stearoyl-CoA Desaturase Inhibitor Reverses α-Synuclein Toxicity.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells.International journal of molecular sciences · 2021Article
- Elongation rate and average length of amyloid fibrils in solution using isotope-labelled small-angle neutron scattering.RSC chemical biology · 2021Article
- Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation.Frontiers in molecular neuroscience · 2021Article
- Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.Nature structural & molecular biology · 2019Article
- Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Comparison of the 3D structures of mouse and human α-synuclein fibrils by solid-state NMR and STEM.Journal of structural biology · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T.International journal of molecular sciences · 2018Article
- A Protofilament-Protofilament Interface in the Structure of Mouse α-Synuclein Fibrils.Biophysical journal · 2018Article
- Non-steric-zipper models for pathogenic α-synuclein conformers.APL bioengineering · 2018Article
- Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy.The Journal of biological chemistry · 2018Article
- Guidelines for using Bsoft for high resolution reconstruction and validation of biomolecular structures from electron micrographs.Protein science : a publication of the Protein Society · 2018Article
- Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.Biophysical journal · 2017Article
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Authors and funding
8 authors at 5 institutions in 4 countries.
Funding
Abstract
Parkinson disease and other progressive neurodegenerative conditions are characterized by the intracerebral presence of Lewy bodies, containing amyloid fibrils of α-synuclein. We used cryo-electron microscopy and scanning transmission electron microscopy (STEM) to study in vitro-assembled fibrils. These fibrils are highly polymorphic. Focusing on twisting fibrils with an inter-crossover spacing of 77 nm, our reconstructions showed them to consist of paired protofibrils. STEM mass per length data gave one subunit per 0.47 nm axial rise per protofibril, consistent with a superpleated β-structure. The STEM images show two thread-like densities running along each of these fibrils, which we interpret as ladders of metal ions. These threads confirmed the two-protofibril architecture of the 77-nm twisting fibrils and allowed us to identify this morphotype in STEM micrographs. Some other, but not all, fibril morphotypes also exhibit dense threads, implying that they also present a putative metal binding site. We propose a molecular model for the protofibril and suggest that polymorphic variant fibrils have different numbers of protofibrils that are associated differently.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.