ArticleThe Journal of biological chemistry2010
Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Clinical translation of fluid, imaging, and digital biomarkers for Alzheimer's disease.Alzheimer's research & therapy · 2026Review
- Optimization of penalization function in Bayesian penalized likelihood reconstruction algorithm for [Physical and engineering sciences in medicine · 2024Article
- Cellular and pathological functions of tau.Nature reviews. Molecular cell biology · 2024Review
- Biophysical Studies of Amyloid-Binding Fluorophores to Tau AD Core Fibrils Formed without Cofactors.International journal of molecular sciences · 2024Article
- A new electrochemical method that mimics phosphorylation of the core tau peptide K18 enables kinetic and structural analysis of intermediates and assembly.The Journal of biological chemistry · 2023Article
- Light Microscopy and Dynamic Light Scattering to Study Liquid-Liquid Phase Separation of Tau Proteins In Vitro.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The intriguing dose-dependent effect of selected amphiphilic compounds on insulin amyloid aggregation: Focus on a cholesterol-based detergent, Chobimalt.Frontiers in molecular biosciences · 2022Article
- Recent advances in cellular biosensor technology to investigate tau oligomerization.Bioengineering & translational medicine · 2021Review
- Role of Microglia in Regulating Cholesterol and Tau Pathology in Alzheimer's Disease.Cellular and molecular neurobiology · 2021Review
- In situ architecture of neuronal α-Synuclein inclusions.Nature communications · 2021Article
- Tau-proximity ligation assay reveals extensive previously undetected pathology prior to neurofibrillary tangles in preclinical Alzheimer's disease.Acta neuropathologica communications · 2021Article
- Tau-PET imaging as a molecular modality for Alzheimer's disease.American journal of nuclear medicine and molecular imaging · 2021Article
- Atomic Force Microscopy Imaging and Nanomechanical Properties of Six Tau Isoform Assemblies.Biophysical journal · 2020Article
- FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments.Molecular neurodegeneration · 2020Article
- Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation.Acta neuropathologica · 2020Article
- Molecular Insight into the Therapeutic Promise of Flavonoids against Alzheimer's Disease.Molecules (Basel, Switzerland) · 2020Review
- Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau.Nature communications · 2020Article
- Anisotropy of Anomalous Diffusion Improves the Accuracy of Differentiating and Grading Alzheimer's Disease Using Novel Fractional Motion Model.Frontiers in aging neuroscience · 2020Article
- Identification and Classification of Alzheimer's Disease Patients Using Novel Fractional Motion Model.Frontiers in neuroscience · 2020Article
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Authors and funding
6 authors.
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Abstract
Fibrous aggregates of Tau protein are characteristic features of Alzheimer disease. We applied high resolution atomic force and EM microscopy to study fibrils assembled from different human Tau isoforms and domains. All fibrils reveal structural polymorphism; the "thin twisted" and "thin smooth" fibrils resemble flat ribbons (cross-section approximately 10 x 15 nm) with diverse twist periodicities. "Thick fibrils" show periodicities of approximately 65-70 nm and thicknesses of approximately 9-18 nm such as routinely reported for "paired helical filaments" but structurally resemble heavily twisted ribbons. Therefore, thin and thick fibrils assembled from different human Tau isoforms challenge current structural models of paired helical filaments. Furthermore, all Tau fibrils reveal axial subperiodicities of approximately 17-19 nm and, upon exposure to mechanical stress or hydrophobic surfaces, disassemble into uniform fragments that remain connected by thin thread-like structures ( approximately 2 nm). This hydrophobically induced disassembly is inhibited at enhanced electrolyte concentrations, indicating that the fragments resemble structural building blocks and the fibril integrity depends largely on hydrophobic and electrostatic interactions. Because full-length Tau and repeat domain constructs assemble into fibrils of similar thickness, the "fuzzy coat" of Tau protein termini surrounding the fibril axis is nearly invisible for atomic force microscopy and EM, presumably because of its high flexibility.
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