ArticleActa neuropathologica communications2013
A central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease.
Article in Acta neuropathologica communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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90 citing papers in PubMed, 178 citations in OpenAlex.
- Spatiotemporal characterization of Alzheimer disease pathology in living human brain tissue.Nature communications · 2026Article
- Micro/Nanoplastics Drive Amyloid‑β Colloidal and Oxidative Reorganization: A Real-World Contaminant Stressor.ACS omega · 2026Article
- The Role of Cytochrome P450 Holoenzyme Metabolism in the Origin of Neuropathologies.International journal of molecular sciences · 2026Review
- Review
- Apelin-13 confers Neuropeptide Y-mediated neuroprotection and preserves learning and allocentric memory in D-glutamic acid-induced excitotoxicity in rats.Molecular neurobiology · 2026Article
- Binding of Hg(I) and Hg(II) Ions to Amyloid-Beta (Aβ) Peptide Variants Affect their Structure and Aggregation.Chembiochem : a European journal of chemical biology · 2025Article
- Redox reactivities of membrane-bound amyloid-β-Cu complexes and their targeting by metallothionein-3.Free radical biology & medicine · 2025Article
- Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression.Chembiochem : a European journal of chemical biology · 2025Review
- Identifying the important involvement of cuproptosis in the pathophysiology of age-related macular degeneration.European journal of medical research · 2025Article
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- A Focus on the Link Between Metal Dyshomeostasis, Norepinephrine, and Protein Aggregation.Antioxidants (Basel, Switzerland) · 2025Review
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases.RSC chemical biology · 2025Review
- Empowering canonical biochemicals with cross-linked novelty: Recursions in applications of protein cross-links.Proteins · 2025Review
- Integrated approach to reducing polypharmacy in older people: exploring the role of oxidative stress and antioxidant potential therapy.Redox report : communications in free radical research · 2024Review
- Crystal Violet Selectively Detects Aβ Oligomers but Not Fibrils In Vitro and in Alzheimer's Disease Brain Tissue.Biomolecules · 2024Article
- Stabilization and Reduced Cytotoxicity of Amyloid Beta Aggregates in the Presence of Catechol Neurotransmitters.Neurochemical research · 2024Article
- Multi-Oxidant Environment as a Suicidal Inhibitor of Myeloperoxidase.Antioxidants (Basel, Switzerland) · 2023Article
- Large-Scale Qualitative and Quantitative Assessment of Dityrosine Crosslinking Omics in Response to Endogenous and Exogenous Hydrogen Peroxide inAntioxidants (Basel, Switzerland) · 2023Article
- Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.Scientific reports · 2023Article
30 more citing papers are in PubMed but not listed here.
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11 authors at 2 institutions in 3 countries.
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Abstract
backgroundAlzheimer's disease (AD) is characterized by the deposition of insoluble amyloid plaques in the neuropil composed of highly stable, self-assembled Amyloid-beta (Aβ) fibrils. Copper has been implicated to play a role in Alzheimer's disease. Dimers of Aβ have been isolated from AD brain and have been shown to be neurotoxic.
resultsWe have investigated the formation of dityrosine cross-links in Aβ42 formed by covalent ortho-ortho coupling of two tyrosine residues under conditions of oxidative stress with elevated copper and shown that dityrosine can be formed in vitro in Aβ oligomers and fibrils and that these links further stabilize the fibrils. Dityrosine crosslinking was present in internalized Aβ in cell cultures treated with oligomeric Aβ42 using a specific antibody for dityrosine by immunogold labeling transmission electron microscopy. Results also revealed the prevalence of dityrosine crosslinks in amyloid plaques in brain tissue and in cerebrospinal fluid from AD patients.
conclusionsAβ dimers may be stabilized by dityrosine crosslinking. These results indicate that dityrosine cross-links may play an important role in the pathogenesis of Alzheimer's disease and can be generated by reactive oxygen species catalyzed by Cu2+ ions. The observation of increased Aβ and dityrosine in CSF from AD patients suggests that this could be used as a potential biomarker of oxidative stress in AD.
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