ArticleAnalytical biochemistry2019
Preparation of stable tau oligomers for cellular and biochemical studies.
Article in Analytical biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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.
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Who cites it
27 citing papers in PubMed.
- 0N4R Tau aggregates producing morphologically different and structurally similar "on-path" and "off-path" oligomers.Chemical communications (Cambridge, England) · 2026Article
- Making tau amyloid models in vitro: a crucial and underestimated challenge.FEBS letters · 2025Review
- Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons.Cell death & disease · 2025Article
- Functional Analysis of Direct In Vitro Effect of Phosphorylated Tau on Mitochondrial Respiration and Hydrogen Peroxide Production.Biomolecules · 2025Article
- Optical signature of retinal Tau fibrillation.Scientific reports · 2025Article
- Tubulin-Binding Region Modulates Cholesterol-Triggered Aggregation of Tau Proteins.Journal of neurochemistry · 2025Article
- Under Heparin-Free Conditions Unsaturated Phospholipids Inhibit the Aggregation of 1N4R and 2N4R Tau.The journal of physical chemistry letters · 2024Article
- Tubulin-binding region alters tau-lipid interactions and changes toxicity of tau fibrils formed in the presence of phosphatidylserine lipids.Protein science : a publication of the Protein Society · 2024Article
- Novel ultrasensitive immunoassay for the selective quantification of tau oligomers and related soluble aggregates.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Functional Applications of Stable Tau Oligomers in Cell Biology and Electrophysiology Studies.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A Validated Method to Prepare Stable Tau Oligomers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Site-Specific C-Terminal Fluorescent Labeling of Tau Protein.ACS omega · 2022Article
- Linking the Amyloid, Tau, and Mitochondrial Hypotheses of Alzheimer's Disease and Identifying Promising Drug Targets.Biomolecules · 2022Review
- Chemico-Pharmacological Screening of the Methanol Extract ofMolecules (Basel, Switzerland) · 2022Article
- Truncating tau reveals different pathophysiological actions of oligomers in single neurons.Communications biology · 2021Article
- The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.The protein journal · 2021Review
- Revealing Intrinsic Disorder and Aggregation Properties of the DPF3a Zinc Finger Protein.ACS omega · 2021Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Increasing evidence suggests that small oligomers are the principal neurotoxic species of tau in Alzheimer's disease and other tauopathies. However, mechanisms of tau oligomer-mediated neurodegeneration are poorly understood. The transience of oligomers due to aggregation can compromise the stability of oligomers prepared in vitro. Consequently, we sought to develop an efficient method which maintains the stability and globular conformation of preformed oligomers. This study demonstrates that labeling a single-cysteine form of the pro-aggregant tau four-repeat region (K18) with either Alexa Fluor 488-C5-maleimide or N-ethylmaleimide in reducing conditions stabilizes oligomers by impeding their further aggregation. Furthermore, the use of this approach to study the propagation of labeled extracellular tau K18 oligomers into human neuroblastoma cells and human stem cell-derived neurons is described. This method is potentially applicable for preparing stabilized oligomers of tau for diagnostic and biomarker tests, as well as for in vitro structure-activity relationship assays.
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