ArticleNature chemistry2017
A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells.
Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Capturing Early Aggregation Transitions of Disordered Tau by Covalent Footprinting Mass Spectrometry.Analytical chemistry · 2026Article
- Macrocyclic β-arch peptides that mimic the structure and function of disease-associated tau folds.Nature chemistry · 2025Article
- Water-directed pinning is key to tau prion formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- dGAE(297-391) Tau Fragment Promotes Formation of Chronic Traumatic Encephalopathy-Like Tau Filaments.Angewandte Chemie (International ed. in English) · 2024Article
- Precision proteoform design for 4R tau isoform selective templated aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation.bioRxiv : the preprint server for biology · 2023Article
- Discovery of Dual Aβ/Tau Inhibitors and Evaluation of Their Therapeutic Effect on aACS chemical neuroscience · 2022Article
- Joint Computational/Cell-Based Approach for Screening Inhibitors of Tau Oligomerization: A Proof-of-Concept Study.Journal of Alzheimer's disease : JAD · 2022Article
- Emergence of distinct and heterogeneous strains of amyloid beta with advanced Alzheimer's disease pathology in Down syndrome.Acta neuropathologica communications · 2021Article
- N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding.ACS chemical neuroscience · 2021Article
- Effects of All-Atom Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of PHF6 Peptide of Tau Protein.Journal of chemical theory and computation · 2021Article
- The potential role of glial cells in driving the prion-like transcellular propagation of tau in tauopathies.Brain, behavior, & immunity - health · 2021Review
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates.Journal of neuropathology and experimental neurology · 2021Review
- Inclusion of the C-Terminal Domain in the β-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy.Journal of the American Chemical Society · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- NMR Studies of Tau Protein in Tauopathies.Frontiers in molecular biosciences · 2021Review
- Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils.Scientific reports · 2020Article
- The Role of Copper in Tau-Related Pathology in Alzheimer's Disease.Frontiers in molecular neuroscience · 2020Review
- Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation.The Journal of biological chemistry · 2019Article
- In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
17 authors.
Funding
Abstract
The self-propagation of misfolded conformations of tau underlies neurodegenerative diseases, including Alzheimer's. There is considerable interest in discovering the minimal sequence and active conformational nucleus that defines this self-propagating event. The microtubule-binding region, spanning residues 244-372, reproduces much of the aggregation behaviour of tau in cells and animal models. Further dissection of the amyloid-forming region to a hexapeptide from the third microtubule-binding repeat resulted in a peptide that rapidly forms fibrils in vitro. We show that this peptide lacks the ability to seed aggregation of tau
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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.