ReviewThe Journal of biological chemistry2019
Elucidating Tau function and dysfunction in the era of cryo-EM.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Digging Deep into Alzheimer Disease: How Electron Microscopy Helps Elucidating Its Pathogenesis.Cellular and molecular neurobiology · 2026Review
- Peptide-Based Therapeutics for Alzheimer's Disease: Medicinal Chemistry, AI-Guided Computational Design, and Blood-Brain Barrier Delivery.Drug design, development and therapy · 2026Review
- Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins · 2025Review
- The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.PNAS nexus · 2024Article
- Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates.Nature communications · 2023Article
- Tau interactome and RNA binding proteins in neurodegenerative diseases.Molecular neurodegeneration · 2022Review
- Role of the Cysteine in R3 Tau Peptide in Copper Binding and Reactivity.International journal of molecular sciences · 2022Article
- Structure-Activity Relationships of Novel Tau Ligands: Passive Fibril Binders and Active Aggregation Inhibitors.ACS chemical biology · 2022Article
- In Silico Analysis of Metabolites from Peruvian Native Plants as Potential Therapeutics against Alzheimer's Disease.Molecules (Basel, Switzerland) · 2022Article
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- It takes more than tau to tangle: using proteomics to determine how phosphorylated tau mediates toxicity in neurodegenerative diseases.Neural regeneration research · 2021Article
- Proteomic Profiling of Extracellular Vesicles Separated from Plasma of Former National Football League Players at Risk for Chronic Traumatic Encephalopathy.Aging and disease · 2021Article
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates.Journal of neuropathology and experimental neurology · 2021Review
- A theoretical study of polymorphism in VQIVYK fibrils.Biophysical journal · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- A novel structure associated with aging is augmented in the DPP6-KO mouse brain.Acta neuropathologica communications · 2020Article
- Risk of Transmissibility From Neurodegenerative Disease-Associated Proteins: Experimental Knowns and Unknowns.Journal of neuropathology and experimental neurology · 2020Review
- The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18.European biophysics journal : EBJ · 2020Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a microtubule-associated protein involved in the regulation of axonal microtubules in neurons. In pathological conditions, it forms fibrils that are molecular hallmarks of neurological disorders known as tauopathies. In the last 2 years, cryo-EM has given unprecedented high-resolution views of Tau in both physiological and pathological conditions. We review here these new findings and put them into the context of the knowledge about Tau before this structural breakthrough. The first structures of Tau fibrils, a molecular hallmark of Alzheimer's disease (AD), were based on fibrils from the brain of an individual with AD and, along with similar patient-derived structures, have set the gold standard for the field. Cryo-EM structures of Tau fibers in three distinct diseases, AD, Pick's disease, and chronic traumatic encephalopathy, represent the end points of Tau's molecular trajectory. We propose that the recent Tau structures may call for a re-examination of databases that link different Tau variants to various forms of dementia. We also address the question of how this structural information may link Tau's functional and pathological aspects. Because this structural information on Tau was obtained in a very short period, the new structures should be viewed in light of earlier structural observations and past and present functional data to shed additional light on Tau function and dysfunction.
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Registered trials
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.