ReviewActa neuropathologica2022
Ultrastructural and biochemical classification of pathogenic tau, α-synuclein and TDP-43.
Review in Acta neuropathologica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers, 1 of them a synthesis that pooled it.
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.
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
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.
- Fluid Biomarkers of Cognitive Impairments Following Traumatic Brain Injury: A Systematic Review and Meta Analysis.International journal of molecular sciences · 2026Pooled it
- Lost in translation: absence of KIAA1324/ELAPOR1 protein in pathological TDP-43-affected neurons in ALS/FTD.Acta neuropathologica communications · 2026Article
- Exploratory assessment of phosphorylated TDP-43 immunoreactivity in minor salivary glands of patients with ALS.Acta neuropathologica communications · 2026Article
- Co-aggregation of annexin A11 and TDP-43 in FTLD/MND with primary lateral sclerosis phenotype.Acta neuropathologica communications · 2026Article
- Moderate Chronic Treadmill Exercise Slows Dopaminergic Neuron Loss in a Rat Model of Parkinson's Disease and Alters RNA Content of Circulating Plasma Exosomes.Journal of neuroscience research · 2025Article
- Advances in PET imaging of protein aggregates associated with neurodegenerative disease.Nature reviews. Neurology · 2025Review
- Argyrophilic Grain Disease Clinically Presenting as Progressive Supranuclear Palsy with Progressive Gait Freezing.Movement disorders clinical practice · 2025Article
- α-Synuclein Pathology in Synucleinopathies: Mechanisms, Biomarkers, and Therapeutic Challenges.International journal of molecular sciences · 2025Review
- Probe-dependent Proximity Profiling (ProPPr) Uncovers Similarities and Differences in Phospho-Tau-Associated Proteomes Between Tauopathies.Molecular neurodegeneration · 2025Article
- Time-course remodeling and pathology intervention of α-synuclein amyloid fibril by heparin and heparin-like oligosaccharides.Nature structural & molecular biology · 2025Article
- Inhibition of Phosphorylated Alpha-Synuclein Aggregation by Synthetic Protein Mimetics and Foldamers.ACS chemical neuroscience · 2025Article
- Argyrophilic grain disease: epidemiology and association with cognitive decline and parkinsonism.Brain communications · 2025Article
- A case of argyrophilic grain disease with an initial clinical diagnosis of Parkinson's disease.Journal of neurology · 2024Article
- USP9X-mediated deubiquitination of Raptor contributes to autophagy impairment and memory deficits in P301S mice.Cell communication and signaling : CCS · 2024Article
- Article
- Pure argyrophilic grain disease revisited: independent effects on limbic, neocortical, and striato-pallido-nigral degeneration and the development of dementia in a series with a low to moderate Braak stage.Acta neuropathologica communications · 2024Article
- Article
- Nonintuitive Immunogenicity and Plasticity of Alpha-Synuclein Conformers: A Paradigm for Smart Delivery of Neuro-Immunotherapeutics.Pharmaceutics · 2024Review
- Novel aspects of the phosphorylation and structure of pathological tau: implications for tauopathy biomarkers.FEBS open bio · 2024Review
- Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent.Current issues in molecular biology · 2024Review
Corrections and comments
- Erratum issued
Authors and funding
11 authors at 10 institutions in 3 countries.
Funding
Abstract
Intracellular accumulation of abnormal proteins with conformational changes is the defining neuropathological feature of neurodegenerative diseases. The pathogenic proteins that accumulate in patients' brains adopt an amyloid-like fibrous structure and exhibit various ultrastructural features. The biochemical analysis of pathogenic proteins in sarkosyl-insoluble fractions extracted from patients' brains also shows disease-specific features. Intriguingly, these ultrastructural and biochemical features are common within the same disease group. These differences among the pathogenic proteins extracted from patients' brains have important implications for definitive diagnosis of the disease, and also suggest the existence of pathogenic protein strains that contribute to the heterogeneity of pathogenesis in neurodegenerative diseases. Recent experimental evidence has shown that prion-like propagation of these pathogenic proteins from host cells to recipient cells underlies the onset and progression of neurodegenerative diseases. The reproduction of the pathological features that characterize each disease in cellular and animal models of prion-like propagation also implies that the structural differences in the pathogenic proteins are inherited in a prion-like manner. In this review, we summarize the ultrastructural and biochemical features of pathogenic proteins extracted from the brains of patients with neurodegenerative diseases that accumulate abnormal forms of tau, α-synuclein, and TDP-43, and we discuss how these disease-specific properties are maintained in the brain, based on recent experimental insights.
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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.