ArticleeLife2022
Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 192 papers.
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Who cites it
192 citing papers in PubMed, 276 citations in OpenAlex.
- Repositioning of polyubiquitin alters the pathologic tau filament structure.Nature structural & molecular biology · 2026Article
- 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
- A proteomic analysis of the PHF-forming tau fragment (tau297-391) following uptake into differentiated human neuronal SHSY5Y cells.Bioscience reports · 2026Article
- Structural Hierarchy and Maturation of Amyloid Fibrils Revealed by Interface Descriptor Analysis.Journal of chemical information and modeling · 2026Article
- Solvent-Isotope Effects in Biomolecular Phase Separation and Fibrillation of Disordered Proteins and Peptides.bioRxiv : the preprint server for biology · 2026Article
- Review
- Protocol for efficient purification of endotoxin-free human recombinant tau protein.STAR protocols · 2026Article
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- A third-generation, high-affinity biparatopic anti-tau antibody inhibits intracellular tau aggregation seeded by Alzheimer's brain extracts.Alzheimer's research & therapy · 2026Article
- NanoBiT screening identifies the azaoxafluorene VT11 as potent tau interaction inhibitor.Scientific reports · 2026Article
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- Water-Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils.Angewandte Chemie (International ed. in English) · 2026Article
- Recent advances in Alzheimer's disease: From molecular mechanisms to therapeutic strategies.Cell · 2026Review
- The Pick fold in tau filaments from human MAPT mutants.Acta neuropathologica · 2026Article
- Structures and Dynamics of Tau Assemblies from Solid-State NMR.Accounts of chemical research · 2026Article
- Spontaneous aging of mature amyloids alters structural stability, cytotoxicity, and susceptibility to biological clearance.Cell death discovery · 2026Article
- The amyloid packing difference: A pairwise comparison metric for amyloid structures.Structure (London, England : 1993) · 2026Article
- Efficient tag-less purification of recombinant human tau proteins.Analytical biochemistry · 2026Article
- Plasma Phosphorylated Tau 217 in Participants at Risk for Chronic Traumatic Encephalopathy.JAMA network open · 2026Article
- Generation of Infectious Prions Amenable to Site-Specific Click Chemistry.ACS chemical biology · 2026Article
132 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Abundant filamentous inclusions of tau are characteristic of more than 20 neurodegenerative diseases that are collectively termed tauopathies. Electron cryo-microscopy (cryo-EM) structures of tau amyloid filaments from human brain revealed that distinct tau folds characterise many different diseases. A lack of laboratory-based model systems to generate these structures has hampered efforts to uncover the molecular mechanisms that underlie tauopathies. Here, we report in vitro assembly conditions with recombinant tau that replicate the structures of filaments from both Alzheimer's disease (AD) and chronic traumatic encephalopathy (CTE), as determined by cryo-EM. Our results suggest that post-translational modifications of tau modulate filament assembly, and that previously observed additional densities in AD and CTE filaments may arise from the presence of inorganic salts, like phosphates and sodium chloride. In vitro assembly of tau into disease-relevant filaments will facilitate studies to determine their roles in different diseases, as well as the development of compounds that specifically bind to these structures or prevent their formation.
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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.