ArticleScientific reports2019
Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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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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
28 citing papers in PubMed, 42 citations in OpenAlex.
- In Vitro Evaluation of Amide-Linked Coumarin Scaffolds for the Inhibition of α‑Synuclein and Tau Aggregation.ACS omega · 2025Article
- Evidence of α-Synuclein/Glucocerebrosidase Dual Targeting by Iminosugar Derivatives.ACS chemical neuroscience · 2025Article
- Biofilm-Associated Amyloid Proteins Linked with the Progression of Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- Exploring the Role of Reactive Oxygen Species in the Pathogenesis and Pathophysiology of Alzheimer's and Parkinson's Disease and the Efficacy of Antioxidant Treatment.Antioxidants (Basel, Switzerland) · 2024Review
- Aquaporin-4 and Parkinson's Disease.International journal of molecular sciences · 2024Review
- Inhibition of Protein Aggregation and Endoplasmic Reticulum Stress as a Targeted Therapy for α-Synucleinopathy.Pharmaceutics · 2023Review
- Per Aspera ad Chaos: Vladimir Uversky's Odyssey through the Strange World of Intrinsically Disordered Proteins.Biomolecules · 2023Article
- FRETing about the details: Case studies in the use of a genetically encoded fluorescent amino acid for distance-dependent energy transfer.Protein science : a publication of the Protein Society · 2023Article
- Review
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Pyrogallol, Corilagin and Chebulagic acid target the "fuzzy coat" of alpha-synuclein to inhibit the fibrillization of the protein.RSC advances · 2022Article
- Precision Medicine in Parkinson's Disease: From Genetic Risk Signals to Personalized Therapy.Brain sciences · 2022Review
- Assessing Nordihydroguaiaretic Acid Therapeutic Effect for Glioblastoma Multiforme.Sensors (Basel, Switzerland) · 2022Article
- Identification of Sclareol As a Natural Neuroprotective CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Challenges in Discovering Drugs That Target the Protein-Protein Interactions of Disordered Proteins.International journal of molecular sciences · 2022Review
- New strategies for fluorescently labeling proteins in the study of amyloids.Current opinion in chemical biology · 2021Review
- Genetic encoding of a highly photostable, long lifetime fluorescent amino acid for imaging in mammalian cells.Chemical science · 2021Article
- Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain.Journal of molecular biology · 2021Article
- α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques.Frontiers in chemistry · 2021Review
- The Role of α-Synuclein Oligomers in Parkinson's Disease.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
23 authors at 9 institutions in 6 countries.
Funding
Abstract
Growing evidence implicates α-synuclein aggregation as a key driver of neurodegeneration in Parkinson's disease (PD) and other neurodegenerative disorders. Herein, the molecular and structural mechanisms of inhibiting α-synuclein aggregation by novel analogs of nordihydroguaiaretic acid (NDGA), a phenolic dibenzenediol lignan, were explored using an array of biochemical and biophysical methodologies. NDGA analogs induced modest, progressive compaction of monomeric α-synuclein, preventing aggregation into amyloid-like fibrils. This conformational remodeling preserved the dynamic adoption of α-helical conformations, which are essential for physiological membrane interactions. Oxidation-dependent NDGA cyclization was required for the interaction with monomeric α-synuclein. NDGA analog-pretreated α-synuclein did not aggregate even without NDGA-analogs in the aggregation mixture. Strikingly, NDGA-pretreated α-synuclein suppressed aggregation of naïve untreated aggregation-competent monomeric α-synuclein. Further, cyclized NDGA reduced α-synuclein-driven neurodegeneration in Caenorhabditis elegans. The cyclized NDGA analogs may serve as a platform for the development of small molecules that stabilize aggregation-resistant α-synuclein monomers without interfering with functional conformations yielding potential therapies for PD and related disorders.
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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.