ArticlePloS one2018
Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Novel ultrasensitive immunoassay for the selective quantification of tau oligomers and related soluble aggregates.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Self-Assembly of Insulin-Derived Chimeric Peptides into Two-Component Amyloid Fibrils: The Role of Coulombic Interactions.The journal of physical chemistry. B · 2023Article
- Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.Molecules (Basel, Switzerland) · 2023Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- Characterization of design grammar of peptides for regulating liquid droplets and aggregates of FUS.Scientific reports · 2021Article
- The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021Review
- Tau-proximity ligation assay reveals extensive previously undetected pathology prior to neurofibrillary tangles in preclinical Alzheimer's disease.Acta neuropathologica communications · 2021Article
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- What is strain in neurodegenerative diseases?Cellular and molecular life sciences : CMLS · 2020Review
- Rescue of degenerating neurons and cells by stem cell released molecules: using a physiological renormalization strategy.Physiological reports · 2019Article
- The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?Acta neuropathologica communications · 2019Review
- Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau Aggregation.Frontiers in molecular neuroscience · 2019Article
- Tau Inclusions in Alzheimer's, Chronic Traumatic Encephalopathy and Pick's Disease. A Speculation on How Differences in Backbone Polarization Underlie Divergent Pathways of Tau Aggregation.Frontiers in neuroscience · 2019Article
- Tau-Cofactor Complexes as Building Blocks of Tau Fibrils.Frontiers in neuroscience · 2019Article
- In vitro generation of tau aggregates conformationally distinct from parent tau seeds of Alzheimer's brain.Prion · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorders including Alzheimer's disease (AD). When amyloid growth is induced by seeding with preformed fibrils assembled from the same protein, structural characteristics of the seed are usually imprinted in daughter generations of fibrils. This so-called conformational memory effect may be compromised when the seeding involves proteins with non-identical sequences leading to the emergence of distinct structural variants of fibrils (amyloid 'strains'). Here, we investigate cross-seeding of full-length human Tau (FL Tau) with fibrils assembled from K18 and K18ΔK280 fragments of Tau in the presence of poly-L-glutamate (poly-Glu) as an enhancer of Tau aggregation. To study cross-seeding between Tau polypeptides and the role of the conformational memory effect in induction of Tau amyloid polymorphism, kinetic assays, transmission electron microscopy, infrared spectroscopy and limited proteolysis have been employed. The fastest fibrillization was observed for FL Tau monomers seeded with preformed K18 amyloid yielding daughter fibrils with unique trypsin digestion patterns. Morphological features of daughter FL Tau fibrils induced by K18 and K18ΔK280 seeds were reminiscent of the mother fibrils (i.e. straight paired fibrils and paired helical filaments (PHFs), respectively) but disappeared in the following generations which became similar to unpaired FL Tau amyloid fibrils formed de novo. The structural evolution observed in our study was accompanied by disappearance of the unique proteolysis profile originated from K18. Our findings may have implications for understanding molecular mechanisms of the emergence and stability of Tau amyloid strains.
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