ArticleJournal of the American Chemical Society2015
Tau Binds to Multiple Tubulin Dimers with Helical Structure.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 58 citations in OpenAlex.
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles.Nature communications · 2024Article
- High-throughput assay exploiting disorder-to-order conformational switches: application to the proteasomal Rpn10:E6AP complex.Chemical science · 2024Article
- Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology.Biomolecules · 2023Review
- Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes.Structure (London, England : 1993) · 2020Article
- Probing IDP Interactions with Membranes by Fluorescence Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Independent tubulin binding and polymerization by the proline-rich region of Tau is regulated by Tau's N-terminal domain.The Journal of biological chemistry · 2019Article
- Impaired tau-microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations.The Journal of biological chemistry · 2019Article
- Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Tau isoform-specific stabilization of intermediate states during microtubule assembly and disassembly.The Journal of biological chemistry · 2019Article
- Electrostatics of Tau Protein by Molecular Dynamics.Biomolecules · 2019Article
- Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit.Structure (London, England : 1993) · 2019Article
- Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding.Angewandte Chemie (International ed. in English) · 2019Article
- Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects.Frontiers in aging neuroscience · 2019Article
- Untangling the Conformational Polymorphism of Disordered Proteins Associated With Neurodegeneration at the Single-Molecule Level.Frontiers in molecular neuroscience · 2019Review
- Molecular Encapsulation Inside Microtubules Based on Tau-Derived Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.Scientific reports · 2018Article
- Near-atomic model of microtubule-tau interactions.Science (New York, N.Y.) · 2018Article
- IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.Current opinion in structural biology · 2018Review
- Physical Biology of Axonal Damage.Frontiers in cellular neuroscience · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Understanding the mechanism by which tau binds to and promotes microtubule (MT) assembly as part of its native function may also provide insight into its loss of function that occurs in neurodegenerative disease. Both mechanistic and structural studies of tau have been hindered by its intrinsic disorder and highly dynamic nature. Here, we combine fluorescence correlation spectroscopy and acrylodan fluorescence screening to study the stoichiometry and structural features of tau-tubulin assemblies. Our results show that tau binds to multiple tubulin dimers, even when MT assembly is inhibited. Moreover, we observe helical structure in the repeat regions of the MT binding domain of tau in the tau-tubulin complex, reflecting partial folding upon binding. Our findings support a role for tau's intrinsic disorder in providing a flexible scaffold for binding tubulin and MTs and a disorder-to-order transition in mediating this important interaction.
Indexed as
Identifiers
What OpenQuestion holds
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.