ArticleActa neuropathologica2023
Mutation ∆K281 in MAPT causes Pick's disease.
Article in Acta neuropathologica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 18 citations in OpenAlex.
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S mutation.Acta neuropathologica · 2026Article
- Cryo-EM structures of biopsy-derived TTR fibrils in hereditary transthyretin amyloidosis.Nature communications · 2026Article
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S Mutation.Research square · 2026Article
- The Pick fold in tau filaments from human MAPT mutants.Acta neuropathologica · 2026Article
- Distinct tau filament folds in familial frontotemporal dementia due to thebioRxiv : the preprint server for biology · 2026Article
- Identification of common variants influencing risk of the three-repeat tauopathy Pick's disease: a genome wide association study.medRxiv : the preprint server for health sciences · 2025Article
- A novelAutophagy · 2025Article
- Making tau amyloid models in vitro: a crucial and underestimated challenge.FEBS letters · 2025Review
- Distinct tau filament folds in human MAPT mutants P301L and P301T.Nature structural & molecular biology · 2025Article
- Tau filaments with the Alzheimer fold in human MAPT mutants V337M and R406W.Nature structural & molecular biology · 2025Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Cryo-EM evidence for a common factor in Alzheimer's and other neurodegenerations.bioRxiv : the preprint server for biology · 2025Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.Communications biology · 2024Article
- Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research.Neuron · 2024Review
- Genetic forms of tauopathies: inherited causes and implications of Alzheimer's disease-like TAU pathology in primary and secondary tauopathies.Journal of neurology · 2024Review
- Tau filaments with the chronic traumatic encephalopathy fold in a case of vacuolar tauopathy with VCP mutation D395G.Acta neuropathologica · 2024Article
- Tau filaments with the Alzheimer fold in cases withbioRxiv : the preprint server for biology · 2024Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.bioRxiv : the preprint server for biology · 2024Article
- Tau and neurodegeneration.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Top 100 most-cited articles on tau protein: a bibliometric analysis and evidence mapping.Frontiers in neuroscience · 2024Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Two siblings with deletion mutation ∆K281 in MAPT developed frontotemporal dementia. At autopsy, numerous inclusions of hyperphosphorylated 3R Tau were present in neurons and glial cells of neocortex and some subcortical regions, including hippocampus, caudate/putamen and globus pallidus. The inclusions were argyrophilic with Bodian silver, but not with Gallyas-Braak silver. They were not labelled by an antibody specific for tau phosphorylated at S262 and/or S356. The inclusions were stained by luminescent conjugated oligothiophene HS-84, but not by bTVBT4. Electron cryo-microscopy revealed that the core of tau filaments was made of residues K254-F378 of 3R Tau and was indistinguishable from that of Pick's disease. We conclude that MAPT mutation ∆K281 causes Pick's disease.
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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.