ArticleScientific reports2019
Differential binding affinity of tau repeat region R2 with neuronal-specific β-tubulin isotypes.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Molecular Insights Into the Differential Binding Affinity of Human Katanin Hexamer for C-Terminal Tails of β-Tubulin Isotypes.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Multi-Target Cardioprotective Potential of Garcinia indica Choisy in Olanzapine-Induced Cardiometabolic Dysregulation: Evidence From Computational and Experimental Insights in H9c2(2-1) Cells.Chemistry & biodiversity · 2026Article
- Computational perspectives on tubulin E-hook structure and mechanisms.Biophysical reports · 2026Review
- 3-O Sulfated Heparan Sulfate (G2) Peptide Ligand Impairs the Infectivity ofBiomolecules · 2025Article
- Unveiling the multifaceted pathogenesis and therapeutic drugs of Alzheimer's disease: A comprehensive review.Heliyon · 2024Review
- Structure challenges in the multivalency of Tau-microtubule interactions.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Design and Computational Analysis of an MMP9 Inhibitor in Hypoxia-Induced Glioblastoma Multiforme.ACS omega · 2023Article
- Phosphorylation of Tau R2 Repeat Destabilizes Its Binding to Microtubules: A Molecular Dynamics Simulation Study.ACS chemical neuroscience · 2023Article
- Computational investigation of benzalacetophenone derivatives against SARS-CoV-2 as potential multi-target bioactive compounds.Computers in biology and medicine · 2022Article
- The Effect of Tau and Taxol on Polymerization of MCF7 Microtubules In Vitro.International journal of molecular sciences · 2022Article
- Elucidating type 2 diabetes mellitus risk factor by promoting lipid metabolism with gymnemagenin: AnFrontiers in pharmacology · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a microtubule-associated protein whose C-terminal domain consisting of four repeat regions R1, R2, R3 and R4 binds to microtubules to stabilize them. In several neurodegenerative diseases, tau detaches from microtubules to form insoluble aggregates leading to tauopathy. Microtubules are made up of αβ tubulin subunits. Seven α-tubulin and nine β-tubulin isotypes have been reported to be present in humans till date. These tubulin isotypes show residue composition variations mainly at C-terminal region and bind to motor proteins and anti-mitotic drugs differently. These tubulin isotypes show tissue specific expression as their relative proportion varies significantly in different type of cells. It is also known that tau binds differently to different cell lines and can either promote or demote microtubule polymerization. However, the relative binding affinity of tau to the different β-tubulin isotypes present in different cell lines is completely unknown. Here, we study relative binding affinity of Tau repeat region R2 to neuronal specific tubulin isotypes βI, βIIb, and βIII using molecular modelling approach. The order of binding energy of tau with tubulin is βIII > βIIb > βI. Our strategy can be potentially adapted to understand differential binding affinity of tau towards β-tubulin isotypes present in other cell lines.
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