ArticleThe Journal of biological chemistry2016
Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations.
Article in The Journal of biological chemistry, 2016. 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.
- DEER of Singly Labelled Proteins to Evaluate Supramolecular Packing of Amyloid Fibrils.bioRxiv : the preprint server for biology · 2025Article
- Making tau amyloid models in vitro: a crucial and underestimated challenge.FEBS letters · 2025Review
- Cellular Uptake of Tau Aggregates Triggers Disulfide Bond Formation in Four-Repeat Tau Monomers.ACS chemical neuroscience · 2025Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- MAP2 caps tau fibrils and inhibits aggregation.The Journal of biological chemistry · 2023Article
- A new electrochemical method that mimics phosphorylation of the core tau peptide K18 enables kinetic and structural analysis of intermediates and assembly.The Journal of biological chemistry · 2023Article
- Protein shapes at the core of chronic traumatic encephalopathy.Nature structural & molecular biology · 2019Article
- The role of annealing and fragmentation in human tau aggregation dynamics.The Journal of biological chemistry · 2019Article
- The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?Acta neuropathologica communications · 2019Review
- Distinct Conformations, Aggregation and Cellular Internalization of Different Tau Strains.Frontiers in cellular neuroscience · 2019Article
- Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms.The Journal of biological chemistry · 2018Article
- Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils.PloS one · 2018Article
- Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017Review
- Strains of Pathological Protein Aggregates in Neurodegenerative Diseases.Discoveries (Craiova, Romania) · 2017Review
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Tau fibrils are pathological aggregates that can transfer between neurons and then recruit soluble Tau monomers by template-assisted conversion. The propagation of different fibril polymorphs is thought to be a contributing factor to phenotypic diversity in Alzheimer disease and other Tauopathies. We found that a homogeneous population of Tau fibrils composed of the truncated version K18 (residues 244-372) gradually converted to a new set of fibril conformers when subjected to multiple cycles of seeding and growth. Using double electron-electron resonance (DEER) spectroscopy, we observed that the distances between spin labels at positions 311 and 328 in the fibril core progressively decreased. The findings were corroborated by changes in turbidity, morphology, and protease sensitivity. Fibrils that were initially formed under stirring conditions exhibited an increased fragility compared with fibrils formed quiescently after multiple cycles of seeding. The quiescently formed fibrils were marked by accelerated growth. The difference in fragility and growth between the different conformers explains how the change in incubation condition could lead to the amplification of a minor subpopulation of fibrils. Under quiescent conditions where fibril breakage is minimal, faster growing fibrils have a selective advantage. The findings are of general importance as they suggest that changes in selective pressures during fibril propagation in the human brain could result in the emergence of new fibril conformers with varied clinicopathological consequences.
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