ArticleBiomolecules2019
Electrostatics of Tau Protein by Molecular Dynamics.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Tau Oligomers Resist Phase Separation.Biomolecules · 2025Article
- Analyses of exon 4a structure reveal the properties of Big tau related to distribution, function and aggregation.Frontiers in molecular neuroscience · 2025Article
- Effects of All-Atom and Coarse-Grained Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of a Tau K18 Monomer.Journal of chemical information and modeling · 2024Article
- Critical Evaluation of Polarizable and Nonpolarizable Force Fields for Proteins Using Experimentally Derived Nitrile Electric Fields.Journal of the American Chemical Society · 2024Article
- Enhancing Conformational Sampling for Intrinsically Disordered and Ordered Proteins by Variational Autoencoder.International journal of molecular sciences · 2023Article
- Investigation of the Structure of Full-Length Tau Proteins with Coarse-Grained and All-Atom Molecular Dynamics Simulations.ACS chemical neuroscience · 2023Article
- Effect of Strain Rate on Single Tau, Dimerized Tau and Tau-Microtubule Interface: A Molecular Dynamics Simulation Study.Biomolecules · 2021Article
- Viscoelastic Response of Neurofilaments: An Atomistic Simulation Approach.Biomolecules · 2021Article
- Mechanical behavior of actin and spectrin subjected to high strain rate: A molecular dynamics simulation study.Computational and structural biotechnology journal · 2021Article
- Tau protein- induced sequestration of the eukaryotic ribosome: Implications in neurodegenerative disease.Scientific reports · 2020Article
- Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.Journal of biosciences · 2020Review
- Dynamical decoration of stabilized-microtubules by Tau-proteins.Scientific reports · 2019Article
- Intrinsically Disordered Proteins in Chronic Diseases.Biomolecules · 2019Article
- Role of Phosphorylation and Hyperphosphorylation of Tau in Its Interaction with βα Dimeric Tubulin Studied from a Bioinformatics Perspective.Avicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a microtubule-associated protein that promotes microtubule assembly and stability. This protein is implicated in several neurodegenerative diseases, including Alzheimer's. To date, the three-dimensional (3D) structure of tau has not been fully solved, experimentally. Even the most recent information is sometimes controversial in regard to how this protein folds, interacts, and behaves. Predicting the tau structure and its profile sheds light on the knowledge about its properties and biological function, such as the binding to microtubules (MT) and, for instance, the effect on ionic conductivity. Our findings on the tau structure suggest a disordered protein, with discrete portions of well-defined secondary structure, mostly at the microtubule binding region. In addition, the first molecular dynamics simulation of full-length tau along with an MT section was performed, unveiling tau structure when associated with MT and interaction sites. Electrostatics and conductivity were also examined to understand how tau affects the ions in the intracellular fluid environment. Our results bring a new insight into tau and tubulin MT proteins, their characteristics, and the structure⁻function relationship.
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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.