ArticleScientific reports2016
The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson's disease.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 85 citations in OpenAlex.
- Protein-Protein Cross-Linking by a DNA Damage-Derived Histone Modification.Journal of the American Chemical Society · 2026Article
- "Coordination of Anle138b to Silver Results in Selective Reduction of a C-terminal truncated Alpha-synuclein Protein and Increased Aggregate Size."bioRxiv : the preprint server for biology · 2025Article
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases.RSC chemical biology · 2025Review
- Small Molecules, α-Synuclein Pathology, and the Search for Effective Treatments in Parkinson's Disease.International journal of molecular sciences · 2024Review
- Review
- Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers.ACS chemical neuroscience · 2023Article
- Dityrosine cross-linking and its potential roles in Alzheimer's disease.Frontiers in neuroscience · 2023Review
- Article
- Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe.International journal of molecular sciences · 2022Article
- Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization.Journal of the American Chemical Society · 2022Article
- Molecular Basis of Small-Molecule Binding to α-Synuclein.Journal of the American Chemical Society · 2022Article
- Article
- Oxidative Crosslinking of Peptides and Proteins: Mechanisms of Formation, Detection, Characterization and Quantification.Molecules (Basel, Switzerland) · 2021Review
- Di-Tyrosine Crosslinking andAntioxidants (Basel, Switzerland) · 2021Article
- Examining the Toxicity of α-Synuclein in Neurodegenerative Disorders.Life (Basel, Switzerland) · 2021Review
- New insights into the mechanisms of age-related protein-protein crosslinking in the human lens.Experimental eye research · 2021Review
- NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Frataxins Emerge as New Players of the Intracellular Antioxidant Machinery.Antioxidants (Basel, Switzerland) · 2021Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Parkinson's disease (PD) is characterized by intracellular, insoluble Lewy bodies composed of highly stable α-synuclein (α-syn) amyloid fibrils. α-synuclein is an intrinsically disordered protein that has the capacity to assemble to form β-sheet rich fibrils. Oxidiative stress and metal rich environments have been implicated in triggering assembly. Here, we have explored the composition of Lewy bodies in post-mortem tissue using electron microscopy and immunogold labeling and revealed dityrosine crosslinks in Lewy bodies in brain tissue from PD patients. In vitro, we show that dityrosine cross-links in α-syn are formed by covalent ortho-ortho coupling of two tyrosine residues under conditions of oxidative stress by fluorescence and confirmed using mass-spectrometry. A covalently cross-linked dimer isolated by SDS-PAGE and mass analysis showed that dityrosine dimer was formed via the coupling of Y39-Y39 to give a homo dimer peptide that may play a key role in formation of oligomeric and seeds for fibril formation. Atomic force microscopy analysis reveals that the covalent dityrosine contributes to the stabilization of α-syn assemblies. Thus, the presence of oxidative stress induced dityrosine could play an important role in assembly and toxicity of α-syn in PD.
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