ArticleThe Journal of biological chemistry2016
Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles.
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 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 55 citations in OpenAlex.
- In situ NMR and integrative proteomics reveal the interaction signature of serum α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Investigating plasma lipid profiles in association with Parkinson's disease risk.NPJ Parkinson's disease · 2025Review
- Lipidic folding pathway of α-Synuclein via a toxic oligomer.Nature communications · 2025Article
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Dual-Targeted Nanodiscs Revealing the Cross-Talk between Osteogenic Differentiation of Mesenchymal Stem Cells and Macrophages.ACS nano · 2023Article
- Crosstalk between neurological, cardiovascular, and lifestyle disorders: insulin and lipoproteins in the lead role.Pharmacological reports : PR · 2022Review
- Article
- Structural and Functional Changes of Reconstituted High-Density Lipoprotein (HDL) by Incorporation of α-synuclein: A Potent Antioxidant and Anti-Glycation Activity of α-synuclein and apoA-I in HDL at High Molar Ratio of α-synuclein.Molecules (Basel, Switzerland) · 2021Article
- The Multiple Roles of Sphingomyelin in Parkinson's Disease.Biomolecules · 2021Review
- Transient Lipid-Protein Structures and Selective Ganglioside Uptake During α-Synuclein-Lipid Co-aggregation.Frontiers in cell and developmental biology · 2021Article
- Cooperative Function of LL-37 and HNP1 Protects Mammalian Cell Membranes from Lysis.Biophysical journal · 2020Article
- Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.Molecules (Basel, Switzerland) · 2020Review
- Unroofing site-specific α-synuclein-lipid interactions at the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils.The journal of physical chemistry letters · 2019Article
- Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation.Chemistry and physics of lipids · 2019Article
- Cooperation of Helix Insertion and Lateral Pressure to Remodel Membranes.Biomacromolecules · 2019Article
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.Biochimica et biophysica acta. Biomembranes · 2018Article
- Lipoprotein Particle Formation by Proapoptotic tBid.Biophysical journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiple neurodegenerative diseases are caused by the aggregation of the human α-Synuclein (α-Syn) protein. α-Syn possesses high structural plasticity and the capability of interacting with membranes. Both features are not only essential for its physiological function but also play a role in the aggregation process. Recently it has been proposed that α-Syn is able to form lipid-protein particles reminiscent of high-density lipoproteins. Here, we present a method to obtain a stable and homogeneous population of nanometer-sized particles composed of α-Syn and anionic phospholipids. These particles are called α-Syn lipoprotein (nano)particles to indicate their relationship to high-density lipoproteins formed by human apolipoproteins in vivo and of in vitro self-assembling phospholipid bilayer nanodiscs. Structural investigations of the α-Syn lipoprotein particles by circular dichroism (CD) and magic angle solid-state nuclear magnetic resonance (MAS SS-NMR) spectroscopy establish that α-Syn adopts a helical secondary structure within these particles. Based on cryo-electron microscopy (cryo-EM) and dynamic light scattering (DLS) α-Syn lipoprotein particles have a defined size with a diameter of ∼23 nm. Chemical cross-linking in combination with solution-state NMR and multiangle static light scattering (MALS) of α-Syn particles reveal a high-order protein-lipid entity composed of ∼8-10 α-Syn molecules. The close resemblance in size between cross-linked in vitro-derived α-Syn lipoprotein particles and a cross-linked species of endogenous α-Syn from SH-SY5Y human neuroblastoma cells indicates a potential functional relevance of α-Syn lipoprotein nanoparticles.
Indexed as
Identifiers
What OpenQuestion holds
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.