ReviewBiochemical Society transactions2025
Structural switching of tubulin in the microtubule lattice.
Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- Dissecting Structural and Functional Determinants of Microtubules Stabilization through Guided Chemical Modulation.Journal of medicinal chemistry · 2026Article
- Review
- CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
- MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin.The EMBO journal · 2026Article
- Taxol exploits molecular switches within tubulin to stabilize microtubules.bioRxiv : the preprint server for biology · 2026Article
- Microtubules in the axon are GDP bound but adopt a stable GTP-like expanded state.Nature structural & molecular biology · 2026Article
- Article
- Mechanical force locally damages, remodels, and stabilizes the lattice of spindle microtubules.Current biology : CB · 2026Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Microtubule (MT) dynamic instability, a cycle of growth, catastrophe, shrinkage and rescue, is driven by the switching of tubulin between two structural states, one stabilised by GTP and the other by GDP. Recent work has uncovered the ancient origins of this structural switch and revealed further fundamental elements of microtubule dynamic instability, whereby switching can be brought about by a range of allosteric effectors, propagate deep within the lattice of assembled MTs, and profoundly affect MT function. Here, we review evidence for structural switching within the MT lattice and discuss current ideas about its mechanisms.
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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.