ArticleThe journal of physical chemistry. B2011
α-Synuclein-induced tubule formation in lipid bilayers.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026Article
- A new look at Hsp70 activity in phosphatidylserine-enriched membranes: chaperone-induced quasi-interdigitated lipid phase.Scientific reports · 2023Article
- Monosialotetrahexosylganglioside Promotes Early Aβ42 Oligomer Formation and Maintenance.ACS chemical neuroscience · 2022Article
- Review
- Reverse engineering Lewy bodies: how far have we come and how far can we go?Nature reviews. Neuroscience · 2021Review
- Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- A Focus on the Beneficial Effects of Alpha Synuclein and a Re-Appraisal of Synucleinopathies.Current protein & peptide science · 2018Review
- Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Interface focus · 2017Review
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017Review
- Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein.Biochimica et biophysica acta · 2016Review
- Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles.The Journal of biological chemistry · 2016Article
- Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.The Journal of biological chemistry · 2015Article
- Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis.Biophysical journal · 2015Article
- Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.Biophysical journal · 2014Article
- Membrane remodeling by α-synuclein and effects on amyloid formation.Journal of the American Chemical Society · 2013Article
- α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.The Journal of biological chemistry · 2013Article
- α-Synuclein oligomers with broken helical conformation form lipoprotein nanoparticles.The Journal of biological chemistry · 2013Article
- On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms.ACS chemical neuroscience · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
α-Synuclein is a presynaptic protein that binds to phospholipid membranes and is involved in the pathogenesis of Parkinson's disease (PD). In this paper, we describe the effects of adding wild-type α-synuclein (WT) and three familial PD mutants (A53T, A30P, and E46K) to membranes containing 15-35 mol % anionic lipid. Tubules were observed to form in the membranes to an extent that depended on the α-synuclein variant, the anionic lipid content, and the protein concentration. For all four variants, tubule formation decreased with increasing anionic lipid content. Tubules were more readily observed with A30P and E46K than with WT or A53T. The results are consistent with a model wherein the helical content of α-synuclein increases with increasing anionic lipid content, and α-synuclein conformers with low helical content have a high propensity to induce tubule formation. This work, combined with previous work from our laboratory (Pandey et al. Biophys. J. 2009, 96, 540), shows that WT adsorption of the protein has deleterious effects on the membrane when the anionic lipid concentration is less than 30 mol % (tubule formation) or greater than 40 mol % (reorganization of the bilayer, clustering of protein).
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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.