ArticleProteins2010
Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed.
- Differences in α-synuclein conformational states in physiologically relevant pH/NaThe Analyst · 2026Article
- Protein structure and coupled solvent dynamics in α-synuclein fibrils under controlled confinement.Biophysical journal · 2026Article
- Is synuclein aggregation a derived or ancestral trait? Ancestral sequence reconstruction uncovers stepwise evolution of synuclein aggregation.bioRxiv : the preprint server for biology · 2025Article
- Physical and Mechanical Properties of Monomeric Alpha-Synuclein Provide Leads to Molecular Function.The journal of physical chemistry. B · 2025Article
- Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2025Article
- High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.Analytical chemistry · 2024Article
- Disease Mechanisms of Multiple System Atrophy: What a Parallel Between the Form of Pasta and the Alpha-Synuclein Assemblies Involved in MSA and PD Tells Us.Cerebellum (London, England) · 2024Review
- Cellular Models of Alpha-Synuclein Aggregation: What Have We Learned and Implications for Future Study.Biomedicines · 2022Review
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Can the lack of fibrillar form of alpha-synuclein in Lewy bodies be explained by its catalytic activity?Mathematical biosciences · 2022Article
- The role of the endolysosomal pathway in α-synuclein pathogenesis in Parkinson's disease.Frontiers in cellular neuroscience · 2022Review
- Alpha-Synuclein and Cognitive Decline in Parkinson Disease.Life (Basel, Switzerland) · 2021Review
- 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
- Purification of Recombinant α-synuclein: A Comparison of Commonly Used Protocols.Biochemistry · 2020Article
- Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview.Life (Basel, Switzerland) · 2020Review
- Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation.The Journal of biological chemistry · 2020Article
- Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.Nature communications · 2020Article
- Effect of Osmolytes on Conformational Behavior of Intrinsically Disordered Protein α-Synuclein.Biophysical journal · 2019Article
- Depicting Conformational Ensembles of α-Synuclein by Single Molecule Force Spectroscopy and Native Mass Spectroscopy.International journal of molecular sciences · 2019Article
- Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Conformational heterogeneity of alpha-synuclein was studied with electrospray ionization mass spectrometry by analyzing protein ion charge state distributions, where the extent of multiple charging reflects compactness of the protein conformations in solution. Although alpha-synuclein lacks a single well-defined structure under physiological conditions, it was found to sample four distinct conformational states, ranging from a highly structured one to a random coil. The compact highly structured state of alpha-synuclein is present across the entire range of conditions tested (pH ranging from 2.5 to 10, alcohol content from 0% to 60%), but is particularly abundant in acidic solutions. The only other protein state populated in acidic solutions is a partially folded intermediate state lacking stable tertiary structure. Another, more compact intermediate state is induced by significant amounts of ethanol used as a co-solvent and appears to represent a partially folded conformation with high beta-sheet content. Protein dimerization is observed throughout the entire range of conditions tested, although only acidic solutions favor formation of highly structured dimers of alpha-synuclein. These dimers are likely to present the earliest stages in protein aggregation leading to globular oligomers and, subsequently, protofibrils.
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.