ArticleNature communications2023
FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Organoids: Key advances, optimization, and technological iterations in their application to neurodegenerative diseases.Neural regeneration research · 2026Article
- The Pick fold in tau filaments from human MAPT mutants.Acta neuropathologica · 2026Article
- Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.Research square · 2026Article
- Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.bioRxiv : the preprint server for biology · 2026Article
- DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.bioRxiv : the preprint server for biology · 2025Article
- Making tau amyloid models in vitro: a crucial and underestimated challenge.FEBS letters · 2025Review
- Structural and functional insights into the selective inhibition of mutant tau aggregation by purpurin and oleocanthal in frontotemporal dementia.Protein science : a publication of the Protein Society · 2025Article
- β-Amyloid induces microglial expression of GPC4 and APOE leading to increased neuronal tau pathology and toxicity.Molecular neurodegeneration · 2025Article
- Intrinsic aggregation and propagation of unmodified tau peptides: R2R3 as a minimal model system.Biophysical journal · 2025Article
- Diverse influences on tau aggregation and implications for disease progression.Genes & development · 2025Review
- Human MAPT knockin mouse models of frontotemporal dementia for the neurodegenerative research community.Cell reports methods · 2025Article
- Hairpin trimer transition state of amyloid fibril.Nature communications · 2024Article
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Ensemble-based design of tau to inhibit aggregation while preserving biological activity.Research square · 2024Article
- Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation.ACS chemical neuroscience · 2023Article
- Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope.PLoS pathogens · 2023Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
Amyloid deposition of the microtubule-associated protein tau is associated with neurodegenerative diseases. In frontotemporal dementia with abnormal tau (FTD-tau), missense mutations in tau enhance its aggregation propensity. Here we describe the structural mechanism for how an FTD-tau S320F mutation drives spontaneous aggregation, integrating data from in vitro, in silico and cellular experiments. We find that S320F stabilizes a local hydrophobic cluster which allosterically exposes the
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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.