ArticleBiochemistry2014
A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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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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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.
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Who cites it
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.
- Application of Graph Theory for Identifying Connectivity Patterns in Human Brain Networks: A Systematic Review.Frontiers in neuroscience · 2019Pooled it
- Dynamic Alterations of Functional Systems in Alzheimer's Disease: A Co-Activation Pattern Analysis.Human brain mapping · 2026Article
- Mapping the Role of Monomer Conformation in the Amyloid Formation of α-Synuclein Splice Variants.Journal of the American Chemical Society · 2025Article
- New insights into translational research in Alzheimer's disease guided by artificial intelligence, computational and systems biology.Acta pharmaceutica Sinica. B · 2025Review
- Conformational Ensemble Dynamics of Intrinsically Disordered Full-Length α- and β-Synuclein Monomers.Journal of chemical information and modeling · 2025Article
- Evaluating conversion from mild cognitive impairment to Alzheimer's disease with structural MRI: a machine learning study.Brain communications · 2025Article
- Impact of Phosphorylation on the Physiological Form of Human alpha-Synuclein in Aqueous Solution.Journal of chemical information and modeling · 2024Article
- Data-driven probabilistic definition of the low energy conformational states of protein residues.NAR genomics and bioinformatics · 2024Article
- O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics.ACS chemical neuroscience · 2024Article
- Brain Region-Specific Expression Levels of Synuclein Genes in an Acid Sphingomyelinase Knockout Mouse Model: Correlation with Depression-/Anxiety-Like Behavior and Locomotor Activity in the Absence of Genotypic Variation.International journal of molecular sciences · 2024Article
- Kisspeptin-10 Rescues Cholinergic Differentiated SHSY-5Y Cells from α-Synuclein-Induced Toxicity In Vitro.International journal of molecular sciences · 2022Article
- α-Synuclein phosphorylation at serine 129 occurs after initial protein deposition and inhibits seeded fibril formation and toxicity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Characterization of Amyloidogenic Peptide Aggregability in Helical Subspace.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- The Role of α-Synuclein in Methamphetamine-Induced Neurotoxicity.Neurotoxicity research · 2021Review
- Simultaneous measurement ofJournal of biomolecular NMR · 2021Article
- Predicting MCI to AD Conversation Using Integrated sMRI and rs-fMRI: Machine Learning and Graph Theory Approach.Frontiers in aging neuroscience · 2021Article
- Analysis of Protein Disorder Predictions in the Light of a Protein Structural Alphabet.Biomolecules · 2020Article
- Role of Tyr-39 for the Structural Features of α-Synuclein and for the Interaction with a Strong Modulator of Its Amyloid Assembly.International journal of molecular sciences · 2020Article
- Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
α-Synuclein is an intrinsically disordered protein whose aggregation is implicated in Parkinson's disease. A second member of the synuclein family, β-synuclein, shares significant sequence similarity with α-synuclein but is much more resistant to aggregation. β-Synuclein is missing an 11-residue stretch in the central non-β-amyloid component region that forms the core of α-synuclein amyloid fibrils, yet insertion of these residues into β-synuclein to produce the βSHC construct does not markedly increase the aggregation propensity. To investigate the structural basis of these different behaviors, quantitative nuclear magnetic resonance data, in the form of paramagnetic relaxation enhancement-derived interatomic distances, are combined with molecular dynamics simulations to generate ensembles of structures representative of the solution states of α-synuclein, β-synuclein, and βSHC. Comparison of these ensembles reveals that the differing aggregation propensities of α-synuclein and β-synuclein are associated with differences in the degree of residual structure in the C-terminus coupled to the shorter separation between the N- and C-termini in β-synuclein and βSHC, making protective intramolecular contacts more likely.
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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.