ArticleJournal of the American Chemical Society2012
Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
70 citing papers in PubMed, 139 citations in OpenAlex.
- A comprehensive application of FiveFold for conformation ensemble-based protein structure prediction.Scientific reports · 2025Review
- Alpha-synuclein fibril structures cluster into distinct classes.Biophysical journal · 2025Review
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Single extracellular vesicle detection assay identifies membrane-associated α-synuclein as an early-stage biomarker in Parkinson's disease.Cell reports. Medicine · 2025Article
- Lipidic folding pathway of α-Synuclein via a toxic oligomer.Nature communications · 2025Article
- Characterization of α-synuclein oligomers formed in the presence of lipid vesicles.Biochemistry and biophysics reports · 2024Article
- α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023Review
- α-Synuclein fibril and synaptic vesicle interactions lead to vesicle destruction and increased lipid-associated fibril uptake into iPSC-derived neurons.Communications biology · 2023Article
- SUMO1 hinders α-Synuclein fibrillation by inducing structural compaction.Protein science : a publication of the Protein Society · 2023Article
- Membrane-induced tau amyloid fibrils.Communications biology · 2023Article
- Untwisted α-Synuclein Filaments Formed in the Presence of Lipid Vesicles.Biochemistry · 2022Article
- α-Synuclein Conformational Plasticity: Physiologic States, Pathologic Strains, and Biotechnological Applications.Biomolecules · 2022Review
- Initiation and progression of α-synuclein pathology in Parkinson's disease.Cellular and molecular life sciences : CMLS · 2022Review
- Plasticity of Membrane Binding by the Central Region of α-Synuclein.Frontiers in molecular biosciences · 2022Article
- Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR.Chemical science · 2021Review
- Monoamine Oxidase-B Inhibition Facilitates α-Synuclein SecretionThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Insights into the molecular mechanism of amyloid filament formation: Segmental folding of α-synuclein on lipid membranes.Science advances · 2021Article
- Amyloid β, α-synuclein and the c subunit of the ATP synthase: Can these peptides reveal an amyloidogenic pathway of the permeability transition pore?Biochimica et biophysica acta. Biomembranes · 2021Review
- Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations.ACS nano · 2021Article
- Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.Molecular neurodegeneration · 2020Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
α-Synuclein (AS) fibrils are the main protein component of Lewy bodies, the pathological hallmark of Parkinson's disease and other related disorders. AS forms helices that bind phospholipid membranes with high affinity, but no atomic level data for AS aggregation in the presence of lipids is yet available. Here, we present direct evidence of a conversion from α-helical conformation to β-sheet fibrils in the presence of anionic phospholipid vesicles and direct conversion to β-sheet fibrils in their absence. We have trapped intermediate states throughout the fibril formation pathways to examine the structural changes using solid-state NMR spectroscopy and electron microscopy. The comparison between mature AS fibrils formed in aqueous buffer and those derived in the presence of anionic phospholipids demonstrates no major changes in the overall fibril fold. However, a site-specific comparison of these fibrillar states demonstrates major perturbations in the N-terminal domain with a partial disruption of the long β-strand located in the 40s and small perturbations in residues located in the "non-β amyloid component" (NAC) domain. Combining all these results, we propose a model for AS fibrillogenesis in the presence of phospholipid vesicles.
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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.