Study Finds Tau Protein Does Not Stabilize Microtubules, Challenges Approach to Treating Alzheimer's
![Site-specific hyperphosphorylation of tau inhibits its fibrillization in vitro, blocks its seeding capacity in cells, and disrupts its microtubule binding; Implications for the native state stabilization of tau | bioRxiv Site-specific hyperphosphorylation of tau inhibits its fibrillization in vitro, blocks its seeding capacity in cells, and disrupts its microtubule binding; Implications for the native state stabilization of tau | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2019/09/18/772046/F9.large.jpg)
Site-specific hyperphosphorylation of tau inhibits its fibrillization in vitro, blocks its seeding capacity in cells, and disrupts its microtubule binding; Implications for the native state stabilization of tau | bioRxiv
![IJMS | Free Full-Text | Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction IJMS | Free Full-Text | Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction](https://www.mdpi.com/ijms/ijms-15-04671/article_deploy/html/images/ijms-15-04671f1.png)
IJMS | Free Full-Text | Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction
![Oligomerization of the microtubule‐associated protein tau is mediated by its N‐terminal sequences: implications for normal and pathological tau action - Feinstein - 2016 - Journal of Neurochemistry - Wiley Online Library Oligomerization of the microtubule‐associated protein tau is mediated by its N‐terminal sequences: implications for normal and pathological tau action - Feinstein - 2016 - Journal of Neurochemistry - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/45216c46-831d-4371-bd8a-14e4393ba713/jnc13604-fig-0008-m.jpg)
Oligomerization of the microtubule‐associated protein tau is mediated by its N‐terminal sequences: implications for normal and pathological tau action - Feinstein - 2016 - Journal of Neurochemistry - Wiley Online Library
![Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules | Langmuir Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules | Langmuir](https://pubs.acs.org/cms/10.1021/acs.langmuir.9b02208/asset/images/medium/la9b02208_0007.gif)
Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules | Langmuir
![Tau protein. (A) In physiological conditions, tau binds to microtubules... | Download Scientific Diagram Tau protein. (A) In physiological conditions, tau binds to microtubules... | Download Scientific Diagram](https://www.researchgate.net/publication/336813255/figure/fig1/AS:817982833975296@1572033713719/Tau-protein-A-In-physiological-conditions-tau-binds-to-microtubules-by-its.png)
Tau protein. (A) In physiological conditions, tau binds to microtubules... | Download Scientific Diagram
![Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases | Nature Reviews Drug Discovery Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases | Nature Reviews Drug Discovery](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fnrd2111/MediaObjects/41573_2007_Article_BFnrd2111_Fig1_HTML.jpg)
Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases | Nature Reviews Drug Discovery
![Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. - Abstract - Europe PMC Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. - Abstract - Europe PMC](https://europepmc.org/articles/PMC2787232/bin/nihms-160375-f0021.jpg)
Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. - Abstract - Europe PMC
![Microtubule lattice spacing governs cohesive envelope formation of tau family proteins | Nature Chemical Biology Microtubule lattice spacing governs cohesive envelope formation of tau family proteins | Nature Chemical Biology](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41589-022-01096-2/MediaObjects/41589_2022_1096_Figa_HTML.png)
Microtubule lattice spacing governs cohesive envelope formation of tau family proteins | Nature Chemical Biology
![Gatekeeper of the Cellular Highway: Study Reveals Novel Behaviors of the Alzheimer's Disease Protein Tau | College of Biological Sciences Gatekeeper of the Cellular Highway: Study Reveals Novel Behaviors of the Alzheimer's Disease Protein Tau | College of Biological Sciences](https://biology.ucdavis.edu/sites/g/files/dgvnsk13361/files/styles/sf_landscape_16x9/public/images/article/Tau-Tangles-College-of-Biological-Sciences-UC-Davis_Page_1.jpg?h=d6378a9e&itok=Va90Dl2O)
Gatekeeper of the Cellular Highway: Study Reveals Novel Behaviors of the Alzheimer's Disease Protein Tau | College of Biological Sciences
Modulating the microtubule–tau interactions in biomotility systems by altering the chemical environment - Integrative Biology (RSC Publishing)
![Normal function of tau protein. Tau protein stabilizes microtubules... | Download Scientific Diagram Normal function of tau protein. Tau protein stabilizes microtubules... | Download Scientific Diagram](https://www.researchgate.net/publication/225294145/figure/fig2/AS:203155875864595@1425447543420/Normal-function-of-tau-protein-Tau-protein-stabilizes-microtubules-through-four-tubulin.png)