ReviewIntrinsically disordered proteins2013
Biophysical characterization of α-synuclein and its controversial structure.
Review in Intrinsically disordered proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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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
33 citing papers in PubMed, 72 citations in OpenAlex.
- Concentration-dependent mutational scanning probes the cellular folding landscape of α-synuclein in yeast.Protein science : a publication of the Protein Society · 2026Article
- Concentration-Dependent Mutational Scanning Probes the Cellular Folding Landscape of α-Synuclein in Yeast.bioRxiv : the preprint server for biology · 2025Article
- DR and SPIT: Statistical approaches for identifying transient structure in intrinsically disordered proteins via NMR chemical shifts.Protein science : a publication of the Protein Society · 2025Article
- Monomers, Dimers, and Oligomers of Pyroglutamate-Modified α-Synuclein Fragments Exhibit Distinct Biophysical Characteristics.ACS chemical neuroscience · 2025Article
- A Perspective on Interdicting in Protein Misfolding for Therapeutic Drug Design: Modulating the Formation of Nonlocal Contacts in α-Synuclein as a Strategy against Parkinson's Disease.The journal of physical chemistry. B · 2024Review
- Article
- Single point mutations at the S129 residue of α-synuclein and their effect on structure, aggregation, and neurotoxicity.Frontiers in chemistry · 2023Article
- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
- The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.Nature communications · 2021Article
- Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time.Journal of visualized experiments : JoVE · 2021Article
- Molecular crowding accelerates aggregation of α-synuclein by altering its folding pathway.European biophysics journal : EBJ · 2021Article
- Similarity of the non-amyloid-β component and C-terminal tail of monomeric and tetrameric alpha-synuclein with 14-3-3 sigma.Computational and structural biotechnology journal · 2021Article
- Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.Molecules (Basel, Switzerland) · 2020Review
- Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra.Journal of biomolecular NMR · 2020Article
- Parkinson's disease: proteinopathy or lipidopathy?NPJ Parkinson's disease · 2020Review
- Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk.Journal of Parkinson's disease · 2020Review
- Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration.Neurobiology of disease · 2019Review
- Entropy and Information within Intrinsically Disordered Protein Regions.Entropy (Basel, Switzerland) · 2019Article
- In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.Proteomics · 2019Review
- Computational insights into the role of α-strand/sheet in aggregation of α-synuclein.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
α-synuclein, a presynaptic protein of poorly defined function, constitutes the main component of Parkinson disease-associated Lewy bodies. Extensive biophysical investigations have provided evidence that isolated α-synuclein is an intrinsically disordered protein (IDP) in vitro. Subsequently serving as a model IDP in numerous studies, α-synuclein has aided in the development of many technologies used to characterize IDPs and arguably represents the most thoroughly analyzed IDP to date. Recent reports, however, have challenged the disordered nature of α-synuclein inside cells and have instead proposed a physiologically relevant helical tetramer. Despite α-synuclein's rich biophysical history, a single coherent picture has not yet emerged concerning its in vivo structure, dynamics, and physiological role(s). We present herein a review of the biophysical discoveries, developments, and models pertinent to the characterization of α-synuclein's structure and analysis of the native tetramer controversy.
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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.