ArticleACS chemical neuroscience2018
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
Article in ACS chemical neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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Who cites it
44 citing papers in PubMed.
- Rapid elongation drives the exceptionally fast aggregation of the most common localized human amyloid medin.Communications chemistry · 2026Article
- Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons.Cell death & disease · 2025Article
- A network-level transport model of tau progression in the Alzheimer's brain.Mathematical medicine and biology : a journal of the IMA · 2025Article
- Co-opting templated aggregation to degrade pathogenic tau assemblies and improve motor function.Cell · 2024Article
- Nanotechnology for tau pathology in Alzheimer's disease.Materials today. Bio · 2024Review
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.Chemical science · 2024Article
- Super-resolution imaging unveils the self-replication of tau aggregates upon seeding.Cell reports · 2023Article
- Prion-like strain effects in tauopathies.Cell and tissue research · 2023Review
- Connectome-based biophysics models of Alzheimer's disease diagnosis and prognosis.Translational research : the journal of laboratory and clinical medicine · 2023Review
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- P301S-hTau acetylates KEAP1 to trigger synaptic toxicity via inhibiting NRF2/ARE pathway: A novel mechanism underlying hTau-induced synaptic toxicities.Clinical and translational medicine · 2022Article
- Molecular mechanisms of amyloid formation in living systems.Chemical science · 2022Review
- Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses.Nature communications · 2022Article
- Mitochondrial ROS control neuronal excitability and cell fate in frontotemporal dementia.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- In vivo rate-determining steps of tau seed accumulation in Alzheimer's disease.Science advances · 2021Article
- Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers.Chembiochem : a European journal of chemical biology · 2021Article
- Article
- Linking Oxidative Stress and Proteinopathy in Alzheimer's Disease.Antioxidants (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The ordered assembly of amyloidogenic proteins causes a wide spectrum of common neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. These diseases share common features with prion diseases, in which misfolded proteins can self-replicate and transmit disease across different hosts. Deciphering the molecular mechanisms that underlie the amplification of aggregates is fundamental for understanding how pathological deposits can spread through the brain and drive disease. Here, we used single-molecule microscopy to study the assembly and replication of tau at the single aggregate level. We found that tau aggregates have an intrinsic ability to amplify by filament fragmentation, and determined the doubling times for this replication process by kinetic modeling. We then simulated the spreading time for aggregates through the brain and found this to be in good agreement with both the observed time frame for spreading of pathological tau deposits in Alzheimer's disease and in experimental models of tauopathies. With this work we begin to understand the physical parameters that govern the spreading rates of tau and other amyloids through the human brain.
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Registered trials
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