ArticleThe Journal of biological chemistry2011
Competing interactions stabilize pro- and anti-aggregant conformations of human Tau.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Initiation and modulation of Tau protein phase separation by the drug suramin.Scientific reports · 2023Article
- The Role of Post-Translational Modifications on the Structure and Function of Tau Protein.Journal of molecular neuroscience : MN · 2022Review
- Viscoelastic damage evaluation of the axon.Frontiers in bioengineering and biotechnology · 2022Article
- Review
- The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.The protein journal · 2021Review
- Effect of Strain Rate on Single Tau, Dimerized Tau and Tau-Microtubule Interface: A Molecular Dynamics Simulation Study.Biomolecules · 2021Article
- Modeling links softening of myelin and spectrin scaffolds of axons after a concussion to increased vulnerability to repeated injuries.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021Review
- NMR Studies of Tau Protein in Tauopathies.Frontiers in molecular biosciences · 2021Review
- Article
- 14-3-3/Tau Interaction and Tau Amyloidogenesis.Journal of molecular neuroscience : MN · 2019Review
- Modeling the Axon as an Active Partner with the Growth Cone in Axonal Elongation.Biophysical journal · 2018Article
- Newfound sex differences in axonal structure underlie differential outcomes from in vitro traumatic axonal injury.Experimental neurology · 2018Article
- Microtubule Polymerization and Cross-Link Dynamics Explain Axonal Stiffness and Damage.Biophysical journal · 2018Article
- Physical Biology of Axonal Damage.Frontiers in cellular neuroscience · 2018Article
- Dimerization and Long-Range Repulsion Established by Both Termini of the Microtubule-Associated Protein Tau.Biochemistry · 2017Article
- The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost.Frontiers in neuroscience · 2016Review
- Mechanical Effects of Dynamic Binding between Tau Proteins on Microtubules during Axonal Injury.Biophysical journal · 2015Article
- Alternative conformations of the Tau repeat domain in complex with an engineered binding protein.The Journal of biological chemistry · 2014Article
- Viscoelasticity of tau proteins leads to strain rate-dependent breaking of microtubules during axonal stretch injury: predictions from a mathematical model.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of Tau into amyloid-like fibrils is a key process in neurodegenerative diseases such as Alzheimer. To understand how natively disordered Tau stabilizes conformations that favor pathological aggregation, we applied single-molecule force spectroscopy. Intramolecular interactions that fold polypeptide stretches of ~19 and ~42 amino acids in the functionally important repeat domain of full-length human Tau (hTau40) support aggregation. In contrast, the unstructured N terminus randomly folds long polypeptide stretches >100 amino acids that prevent aggregation. The pro-aggregant mutant hTau40ΔK280 observed in frontotemporal dementia favored the folding of short polypeptide stretches and suppressed the folding of long ones. This trend was reversed in the anti-aggregant mutant hTau40ΔK280/PP. The aggregation inducer heparin introduced strong interactions in hTau40 and hTau40ΔK280 that stabilized aggregation-prone conformations. We show that the conformation and aggregation of Tau are regulated through a complex balance of different intra- and intermolecular interactions.
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Registered trials
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.