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Multivalency in Tau–Microtubule interactions: Heterogeneous association and functional implications

https://doi.org/10.2139/ssrn.5437999
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07870.xopenalex-snapshot
Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.
inferredcites →https://doi.org/10.1002/jnr.490300116openalex-snapshot
Differences in the abilities of human tau isoforms to promote microtubule assembly
inferredcites →https://doi.org/10.1007/978-1-4614-0659-4_1openalex-snapshot
Fuzzy Complexes: A More Stochastic View of Protein Function
inferredcites →https://doi.org/10.1016/0896-6273(89)90210-9openalex-snapshot
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
inferredcites →https://doi.org/10.1016/j.bpj.2017.05.006openalex-snapshot
Heterogeneous Tau-Tubulin Complexes Accelerate Microtubule Polymerization
inferredcites →https://doi.org/10.1016/j.febslet.2015.07.022openalex-snapshot
Fuzzy complexes: Specific binding without complete folding
inferredcites →https://doi.org/10.1016/j.jmb.2009.08.010openalex-snapshot
Nonnative Electrostatic Interactions Can Modulate Protein Folding: Molecular Dynamics with a Grain of Salt
inferredcites →https://doi.org/10.1016/j.jmb.2021.166988openalex-snapshot
Modulating Microtubules: A Molecular Perspective on the Effects of Tail Modifications
inferredcites →https://doi.org/10.1016/j.jsb.2006.11.010openalex-snapshot
Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
inferredcites →https://doi.org/10.1016/j.tibs.2007.10.003openalex-snapshot
Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
inferredcites →https://doi.org/10.1016/s0021-9258(19)51080-8openalex-snapshot
Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.
inferredcites →https://doi.org/10.1021/acs.biochem.3c00092openalex-snapshot
It Takes Tau to Tango: Investigating the Fuzzy Interaction between the R2-Repeat Domain and Tubulin C-Terminal Tails
inferredcites →https://doi.org/10.1021/acs.jpcb.0c11479openalex-snapshot
A Data-Driven Hydrophobicity Scale for Predicting Liquid–Liquid Phase Separation of Proteins
inferredcites →https://doi.org/10.1021/acschemneuro.2c00611openalex-snapshot
Phosphorylation of Tau R2 Repeat Destabilizes Its Binding to Microtubules: A Molecular Dynamics Simulation Study
inferredcites →https://doi.org/10.1021/bi0493160openalex-snapshot
Tau Induces Ring and Microtubule Formation from αβ-Tubulin Dimers under Nonassembly Conditions
inferredcites →https://doi.org/10.1021/jacs.5b04561openalex-snapshot
Tau Binds to Multiple Tubulin Dimers with Helical Structure
inferredcites →https://doi.org/10.1038/34465openalex-snapshot
Structure of the αβ tubulin dimer by electron crystallography
inferredcites →https://doi.org/10.1038/s41598-019-48790-1openalex-snapshot
Dynamical decoration of stabilized-microtubules by Tau-proteins
inferredcites →https://doi.org/10.1073/pnas.1315983111openalex-snapshot
Tau mutants bind tubulin heterodimers with enhanced affinity
inferredcites →https://doi.org/10.1073/pnas.1504081112openalex-snapshot
Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
inferredcites →https://doi.org/10.1073/pnas.1633508100openalex-snapshot
Differential regulation of microtubule dynamics by three- and four-repeat tau: Implications for the onset of neurodegenerative disease
inferredcites →https://doi.org/10.1073/pnas.1914772117openalex-snapshot
Tubulin tails and their modifications regulate protein diffusion on microtubules
inferredcites →https://doi.org/10.1073/pnas.72.5.1858openalex-snapshot
A protein factor essential for microtubule assembly.
inferredcites →https://doi.org/10.1074/jbc.m002590200openalex-snapshot
Nonsaturable Binding Indicates Clustering of Tau on the Microtubule Surface in a Paired Helical Filament-like Conformation
inferredcites →https://doi.org/10.1074/jbc.m007489200openalex-snapshot
Structural and Functional Differences between 3-Repeat and 4-Repeat Tau Isoforms
inferredcites →https://doi.org/10.1074/jbc.m112.364067openalex-snapshot
Tau Isoform Composition Influences Rate and Extent of Filament Formation
inferredcites →https://doi.org/10.1074/jbc.m112.369785openalex-snapshot
Tau Protein Diffuses along the Microtubule Lattice
inferredcites →https://doi.org/10.1074/jbc.m607159200openalex-snapshot
The “Jaws” of the Tau-Microtubule Interaction
inferredcites →https://doi.org/10.1074/jbc.ra119.010172openalex-snapshot
Independent tubulin binding and polymerization by the proline-rich region of Tau is regulated by Tau's N-terminal domain
inferredcites →https://doi.org/10.1083/jcb.201711182openalex-snapshot
Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs
inferredcites →https://doi.org/10.1091/mbc.8.2.353openalex-snapshot
Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly.
inferredcites →https://doi.org/10.1126/science.aat1780openalex-snapshot
Near-atomic model of microtubule-tau interactions
inferredcites →https://doi.org/10.1186/s40478-018-0557-6openalex-snapshot
Phosphorylation of different tau sites during progression of Alzheimer’s disease
inferredcites →https://doi.org/10.1371/journal.pbio.1000034openalex-snapshot
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
inferredcites →https://doi.org/10.1523/jneurosci.1490-09.2010openalex-snapshot
Differential Effects of Tau on the Integrity and Function of Neurons Essential for Learning in Drosophila
inferredcites →https://doi.org/10.3389/fmolb.2021.761227openalex-snapshot
NMR Studies of Tau Protein in Tauopathies
inferredcites →https://doi.org/10.3389/fneur.2020.590059openalex-snapshot
Much More Than a Cytoskeletal Protein: Physiological and Pathological Functions of the Non-microtubule Binding Region of Tau
inferredcites →https://doi.org/10.3389/fnins.2021.643115openalex-snapshot
Differential Effects of the Six Human TAU Isoforms: Somatic Retention of 2N-TAU and Increased Microtubule Number Induced by 4R-TAU
inferredcites →https://doi.org/10.3390/biom12111573openalex-snapshot
Proline-Rich Region II (PRR2) Plays an Important Role in Tau–Glycan Interaction: An NMR Study
inferredcites →https://doi.org/10.3390/ijms150814697openalex-snapshot
Quantitative Analysis of Tau-Microtubule Interaction Using FRET
inferredcites →https://doi.org/10.3390/molecules28114544openalex-snapshot
Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status
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