ArticleProtein science : a publication of the Protein Society2022
Three-repeat and four-repeat tau isoforms form different oligomers.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
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- Transient Interactions of α-Synuclein N- and C-Termini.ACS chemical neuroscience · 2026Article
- Tau in Alzheimer's disease: Shaping the future patient journey.The journal of prevention of Alzheimer's disease · 2026Review
- Allosteric Modulation of Pathological Ataxin-3 Aggregation: A Path to Spinocerebellar Ataxia Type-3 Therapies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Tau-Mitochondria Interactions in Neurodegeneration: Mechanisms and Therapeutic Potential.Cellular and molecular neurobiology · 2025Review
- Strain-Distinct α-Synuclein and Tau Cross-Seeding Uncovered by Correlative Approach with Optical Photothermal Infrared Sub-Micron Imaging.Journal of the American Chemical Society · 2025Article
- Application of modular isoxazoline-βiScience · 2025Article
- Phosphorylation-Induced Self-Coacervation versus RNA-Assisted Complex Coacervation of Tau Proteins.Journal of the American Chemical Society · 2025Article
- High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.Analytical chemistry · 2024Article
- Diagnosis and Management of Progressive Corticobasal Syndrome.Current treatment options in neurology · 2024Article
- Ligand-based design of [Nature communications · 2024Article
- Lung endothelium, tau, and amyloids in health and disease.Physiological reviews · 2024Review
- Tau seed amplification assay reveals relationship between seeding and pathological forms of tau in Alzheimer's disease brain.Acta neuropathologica communications · 2023Article
- Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers.ACS chemical neuroscience · 2023Article
- Hexameric Aggregation Nucleation Core Sequences and Diversity of Pathogenic Tau Strains.Pathogens (Basel, Switzerland) · 2022Article
- Three-repeat and four-repeat tau isoforms form different oligomers.Protein science : a publication of the Protein Society · 2022Article
- Selective Detection of Misfolded Tau From Postmortem Alzheimer's Disease Brains.Frontiers in aging neuroscience · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Different tauopathies are characterized by the isoform-specific composition of the aggregates found in the brain and by structurally distinct tau strains. Although tau oligomers have been implicated as important neurotoxic species, little is known about how the primary structures of the six human tau isoforms affect tau oligomerization because the oligomers are metastable and difficult to analyze. To address this knowledge gap, here, we analyzed the initial oligomers formed by the six tau isoforms in the absence of posttranslational modifications or other manipulations using dot blots probed by an oligomer-specific antibody, native-PAGE/western blots, photo-induced cross-linking of unmodified proteins, mass-spectrometry, and ion-mobility spectroscopy. We found that under these conditions, three-repeat (3R) isoforms are more prone than four-repeat (4R) isoforms to form oligomers. We also tested whether known inhibitors of tau aggregation affect its oligomerization using three small molecules representing different classes of tau aggregation inhibitors, Methylene Blue (MB), the molecular tweezer CLR01, and the all-D peptide TLKIVW, for their ability to inhibit or modulate the oligomerization of the six tau isoforms. Unlike their reported inhibitory effect on tau fibrillation, the inhibitors had little or no effect on the initial oligomerization. Our study provides novel insight into the primary-quaternary structure relationship of human tau and suggests that 3R-tau oligomers may be an important target for future development of compounds targeting pathological tau assemblies.
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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 Socratic graph.